Satoh, Takanori, Shinoda, Hiroshi, Ishii, Keisuke, Koyama, Masayuki, Sakurai, Nobuhiko, Kaji, Hiroyuki, ...
The complete primary structure of inorganic pyrophosphatase [EC 3.6.1.1] from Bacillus stearothermophilus (ATCC 12016) was determined at the amino acid level by automated Edman degradation. The...
Irie, Masachika, Ohgi, Kazuko, Iwama, Masanori, Koizumi, Machiko, Sasayama, Etsuko, Harada, Kishiko, ...
In order to study the reaction mechanism of RNase Rh from Rhizopus niveus, the rates of cleavage of four 2′3′-cyclic nucleotides by mutant enzymes of RNase Rh, H46F, H109F, E105Q, and K108L were...
Enzymatic Properties of Mutant Forms of RNase Rh from Rhizopus niveus as to Asp51 (1996)
Ohgi, Kazuko, Takeuchi, Mitsuaki, Iwama, Masanori, Irie, Masachika
In order to determine the role of Asp51 of RNase Rh from Rhizopus nimus, enzymes with mutations at the 51st position, D51N,D51E,D51Q, D51S,D51T,D51A,and D51K, were prepared, and their enzymatic...
Enzymatic Properties of Mutant Enzymes at Trp49 and Tyr57 of RNase Rh from Rhizopus niveus (1996)
Ohgi, Kazuko, Takeuchi, Mitsuaki, Iwama, Masanori, Irie, Masachika
In order to establish the role of Tyr57 and Trp49 in the enzymatic reaction of RNase Rh, several mutant enzymes at Tyr57 and Trp49 were prepared by protein engineering and their enzymatic properties...
Role of Lys108 in the Enzymatic Activity of RNase Rh from Rhizopus niveus (1995)
Ohgi, Kazuko, Iwama, Masanori, Tada, Kuriko, Takizawa, Ritsue, Irie, Masachika
In order to elucidate on the mechanism of action of RNase Rh from Rhizopus niveus, we investigated the role of Lys108, which is conserved among the RNase T2 family RNases except for two cases. The...
Nomura, Hideyuki, Inokuchi, Norio, Kobayashi, Hiroko, Koyama, Takashi, Iwama, Masanori, Ohgi, Kazuko, ...
A guanine nucleotide-specific RNase (RNase Po1) was isolated from caps of the fruit bodies of Pleurotus ostreatus. RNase Po1 is most active towards RNA at pH 8.0. The effect of heating on the molar...
Irie, Masachika, Ohgi, Kazuko, Watanabe, Hideaki, Iwama, Masanori, Nakamura, Kazuo T., Kurihara, Hiroyuki, ...
In order to elucidate the mechanism of action of Rhizopus niveus RNase Rh, we investigated the pH profiles of the kinetic parameters of RNase RNAP Rh, a derivative of RNase Rh, and its mutant...
Inokuchi, Norio, Koyama, Takashi, Sawada, Fumio, Irie, Masachika
Two ribonucleases (RNase Phya and RNase Phyb) were purified to homogeneity on SDS-PAGE from the culture filtrate of the fungus Physarum polycephalum. The apparent molecular weights of RNases Phya and...
Role of Asp51 and GlulO5 in the Enzymatic Activity of a Ribonuclease from Rhizopus niveus (1993)
Ohgi, Kazuko, Horiuchi, Hiroyuki, Watanabe, Hideaki, Iwama, Masanori, Takagi, Masamichi, Irie, Masachika
The active site of a base non-specific RNase from Rhizopus niveus (RNase Rh), consists of three histidine residues and one carboxyl group [Ohgi, K. et al. (1992) J. Biochem. 111, 132–138]. In order...
Watanabe, Hideaki, Narumi, Hiroaki, Inaba, Tomio, Ohgi, Kazuko, Irie, Masachika
A ribonuclease (RNase Oy) was purified to homogeneity on SDS-PAGE from the homogenate of oyster (Crussdstrea grigus). The apparent molecular weight estimated from SDS-PAGE was ca. 28 kDa. The pH...
Ohgi, Kazuko, Horiuchi, Hiroyuki, Watanabe, Hideaki, Iwama, Masanori, Takagi, Masamichi, Irie, Masachika
In order to study the structure-function relationship of an RNase T2 family enzyme, RNase Rh, from Rhizopus niveus, we investigated the roles of three histidine residues by means of site-specific...
Ohgi, Kazuko, Horiuchi, Hiroyuki, Watanabe, Hideaki, Takagi, Masamichi, Yano, Keiji, Irie, Masachika
The full-length cDNA encoding RNase Rh, which is secreted extracellularly by Rhizopus niveus, was isolated and its nucleotide sequence was determined. It was placed under control of the promoter of...
Okabe, Yukie, Katayama, Naoko, Iwama, Masanori, Watanabe, Hideaki, Ohgi, Kazuko, Irie, Masachika, ...
Two lectins with RNase activity obtained from eggs of Rana catesbeiana and R. japonica and RNase obtained from R. catesbeiana liver show 65–83% protein homology. The base specificity of these frog...
Inada, Yoichi, Watanabe, Hideaki, Ohgi, Kazuko, Irie, Masachika
In order to elucidate the structure-function relationship of RNases belonging to the RNase T2 family (base non-specific and adenylic acid-preferential RNase), an RNase of this family was purified...
Primary Structure of an Alkaline Ribonuclease from Bovine Liver (1990)
Hosoya, Kenji, Nagareda, Yasuo, Hasemi, Shuichi, Sanda, Akihiro, Takizawa, Yoshio, Watanabe, Hideaki, ...
A pyrimidine base specific and most basic alkaline RNase named RNase BL4 was isolated from bovine liver as a protein showing a single band on slab gel-electrophoresis. The enzyme is most active at pH...
Watanabe, Hideaki, Naitoh, Akiko, Suyama, Yuka, Inokuchi, Norio, Shimada, Hiroko, Koyama, Takashi, ...
The complete primary structure of a base non-specific and adenylic acid preferential RNase (RNase M) from Aspergillus saitoi was determined. The sequence was determined by analysis of the peptides...
Irie, Masachika, Ohgi, Kazuko, Nitta, Reiko, Ikeda, Miyuki, Ueno, Motoko
The difference spectra obtained upon the addition of nucleotides to bovine kidney RNase, which shows 40% sequence homology with bovine pancreatic RNase, are markedly different from those of bovine...
Primary Structure of a Ribonuclease from Bullfrog (Rana catesbeiana) Liver (1989)
Nitta, Reiko, Katayama, Naoko, Okabe, Yukie, Iwama, Masanori, Watanabe, Hideaki, Abe, Yasuko, ...
A pyrimidine base-specific ribonuclease was purified from bullfrog (Rana catesbeiana) liver by means of CM-cellulose column chromatography and affinity chromatography on heparin-Sepharose CL-6B,...
Primary Structure of a Base Non-Specific Ribonuclease from Rhizopus niveus (1988)
Horiuchi, Hiroyuki, Yanai, Koji, Takagi, Masamichi, Yano, Keiji, Wakabayashi, Eiji, Sanda, Akihiro, ...
The primary structure of a base non-specific ribonuclease from Rhizopus niveus (RNase Rh) was determined by nucleotide sequence analysis of the DNA fragment encoding RNase Rh gene including signal...
Primary Structure of a Non-Secretory Ribonuclease from Bovine Kidney (1988)
Irie, Masachika, Nitta, Reiko, Ohgi, Kazuko, Niwata, Yasushi, Watanabe, Hideaki, Iwama, Masanori, ...
The primary structure of a non-secretory ribonuclease from bovine kidney (RNase K2 was determined. The sequence determined was...
The Carbohydrate Moieties of Human Urinary Ribonuclease UL (1987)
HITOI, Akira, YAMASHITA, Katsuko, NIWATA, Yasushi, IRIE, Masachika, KOCHIBE, Naohisa, KOBATA, Akira
Ribonuclease UL. purified from pooled human urine contains approximately 20.7% of neutral sugar and 7.8% of aminosugar. All sugars were quantitatively released as oligosaccharides on...
Site of Alkylation of the Major Ribonuclease from Aspergillus saitoi with Iodoacetate (1986)
IRIE, Masachika, WATANABE, Hideaki, OHGI, Kazuko, HARADA, Masatomi
A base non-specific and adenylic acid preferential ribonuclease from Aspergillus saitoi (RNase M) was modified by [14C]iodoacetic acid. RNase M was inactivated with concomitant incorporation of about...
Distribution of Two Urinary Ribonuclease-Like Enzymes in Human Organs and Body Fluids (1986)
MORITA, Toru, NIWATA, Yasushi, OHGI, Kazuko, OGAWA, Michio, IRIE, Masachika
In order to determine the distribution of two human urinary RNase (RNase Us and RNase UL)-like enzymes in human tissues and body fluids, enzyme immunoassay systems were established using rabbit...
IRIE, Masachika, OHGI, Kazuko, YOSHINAGA, Makiko, YANAGIDA, Tamami, OKADA, Yoshio, TENO, Naoki
1) In order to investigate the roles of Lys1 and Lys7 of RNase A in the enzymatic activity, four S-peptide derivatives were prepared and their abilities to activate S-protein were measured. They are...
Different Behavior towards Raw Starch of Three Forms of Glucoamylase from a Rhizopus Sp. (1985)
TAKAHASHI, Tomoko, KATO, Keiko, IKEGAMI, Yoshio, IRIE, Masachika
Three forms of glucoamylase [EC 3.2.1.3] of a Rhizopus sp., Gluc1 (M.W. 74,000), Gluc2 (M.W. 58,600), and Gluc3 (M.W. 61,400), which have similar pH optima and specific activities towards soluble...
IWAMA, Masanori, TAKAHASHI, Tomoko, INOKUCHI, Norio, KOYAMA, Takashi, IRIE, Masachika
The mechanism of inhibition of the two glucoamylases from a Rhizopus sp. and Aspergillus saitoi by aminoalcohol derivatives was investigated. 1. Hydrolysis of maltose by the glucoamylases was...
WATANABE, Hideaki, ANDO, Eiichi, OHGI, Kazuko, IRIE, Masachika
In order to estimate the size of the active site of guanylic acid specific R Nases (R Nase T1 from Aspergillus oryzae and R Nase St from Streptomyces erythreus) and guanine preferential R Nase (R...
KOYAMA, Takashi, INOKUCHI, Norio, IWAMA, Masanori, IRIE, Masachika
1. In order to elucidate the structure-function relationship of glucoamylases [EC 3.2.1.3, α-D-(1–4)-glucan glucohydrolase] from Aspergillus saitoi, the reaction of a minor component, Glue M2 with...
Purification and Properties of Bovine Kidney Ribonucleases (1985)
NIWATA, Yasushi, OHGI, Kazuko, SANDA, Akihiro, TAKIZAWA, Yoshio, IRIE, Masachika
Two RNases (RNases K1 and K2) were purified from bovine kidney by means of column chromatography on phospho-cellulose, Sephadex G-50, CM-cellulose, heparin-Sepharose, and Agarose-APUP. They were...
SANDA, Akihiro, TAKIZAWA, Yoshio, IWAMA, Masanori, IRIE, Masachika
The carboxyl group in a ribonuclease from Rhizopus sp. (RNase Rh) was modified by a water-soluble carbodiimide, 1-cyclohexyl-3-(2-morpholinyl-(4)-ethyl)carbodiimide p-toluenesulfonate (CMC). From...
IRIE, Masachika, MIKAMI, Fumiko, MONMA, Kumiko, OHGI, Kazuko, WATANABE, Hideaki, YAMAGUCHI, Ryoji, ...
Kinetic parameters, Km and Vmax for the transesterification of oligouridylic acid, (Up)nU> p (n = 0–4), by RNase A were measured spectrophotometrically at pH 7.0 and 25°C. The kinetic...
IWAMA, Maswanori, OHTSUKI, Ritsuko, TAKASHI, Tomoko, IRIE, Masachika
To investigate the role of carboxyl groups of glucoamylases [EC 3.2.1.3] from a Rhizopus sp. (Gluc1 and Gluc2), the modification of Gluc1 and Gluc2with a water-soluble carbodiimide, 1...
IRIE, Masachika, WATANABE, Hideaki, OHGI, Kazuko, TOBE, Mayumi, MATSUMURA, Go, ARATA, Yoji, ...
In order to clarify the subsite structure of ribonuclease A (RNase A), the interactions of pdTp, pAp, dTpdAp, and pdTpdAp with RNase A were investigated by means of kinetic studies and 31P NMR...
OHGI, Kazuko, WATANABE, Hideaki, TAKIZAWA, Mayumi, KIMURA, Yoshie, MATSUTANI, Koichi, KAKINUMA, Etsuko, ...
Two forms of RNases (RNase MLL and RNase MM) from Aspergillus saitoi which are base non-specific and adenylic acid preferential were separated from each other by DEAE-cellulose column chromatography....
KUMAGAI, Hiroshi, YOSHIHARA, Keiko, UMEMOTO, Mitsue, IGARASHI, Kazuei, HIROSE, Seiyu, OHGI, Kazuko, ...
Three alkaline ribonucleases [EC 3.1.4.221 were purified 4,500- to 7,850-fold from bovine parotid gland by repeated CM-Sephadex C-25 chromatography and Sephadex G-50 gel filtration, with a total...
WATANABE, Hideaki, SUGIYAMA, Kazuhito, IWAMA, Masanori, FUTAKI, Reiji, IRIE, Masachika
In order to investigate the role of carboxyl groups of a base non-specific ribonuclease from Aspergillus saitoi [EC 3.1.27.1] (RNase M, molecular weight 36,000), the modification of RNase M with a...
Primary Structure of a Minor Ribonuclease from Aspergillus saitoi (1982)
WATANABE, Hideaki, OHGI, Kazuko, IRIE, Masachika
1. RNase Ms, a base non-specific RNase from Aspergillus saitoi was reduced and carboxymethylated (RCM-RNase Ms). RCM-RNase Ms was hydrolyzed with tryp-sin, and the trypsin digests were then treated...
N-Bromosuccinimide Oxidation of a Glucoamylase from Aspergillus saitoi (1982)
INOKUCHI, Norio, TAKAHASHI, Tomoko, YOSHIMOTO, Akio, IRIE, Masachika
1. In order to elucidate the structure-function relation of a glucoamylase [EC 3.2.1.3, α-D-(1→4) glucan glucohydrolase] from Aspergillus saitoi (Glue M1), the reaction of Gluc M1 with NBS was...
TAKAHASHI, Tomoko, TSUCHIDA, Yukiko, IRIE, Masachika
Two inactive fragments of glucoamylase [EC 3.2.1.3] from a Rhizopus sp. were isolated from the glucoamylase fraction obtained by CM-Sephadex chromatography in the previous purification of the...
INOKUCHI, Norio, IWAMA, Masanori, TAKAHASHI, Tomoko, IRIE, Masachika
In order to elucidate the structure-function relation of a glucoamylase [EC 3.2.1.3, α-D-(1→4)-glucan glucohydrolase] from Aspergillus saitoi (Gluc M1), the reaction of Gluc M1 with water-soluble...
Purification and Characterization of a Minor Glucoamylase from Aspergillus saitoi (1981)
INOKUCHI, Norio, TAKAHASHI, Tomoko, IRIE, Masachika
1. From a digestive produced from Aspergillus saitoi, a minor glucoamylase[EC 3.2.1.3] named Gluc M2 was purified in a yield of 67percnt;, besides a major glucoamylase named Gluc M1 (M.W. 90,000)...
Alkylation of a Ribonuclease from Streptomyces erythreus with Iodoacetate and Iodoacetamide (1981)
OHGI, Kazuko, WATANABE, Hideaki, EMMAN, Kiyoshi, YOSHIDA, Nobuo, IRIE, Masachika
1. RNase St was inactivated by iodoacetate. The inactivation was most rapid at pH 5.0-7.0. Competitive inhibitors protected RNase St from inactivation by iodoacetate. The protective effect of...
Purification and Properties of Human Urine Ribonuclueases (1981)
IWAMA, Masanori, KUNIHIRO, Motoko, OHGI, Kazuko, IRIE, Masachika
1. Two RNases (RNase UL and RNase US) were purified from the urine of human adults by means of column chromatographies on SP-Sephadex C-50, phospho-cel-lulose and CM-cellulose and gel-filtration on...
Purification and Characterization of a Glucoamylase from Aspergillus saitoi (1981)
TAKAHASHI, Tomoko, INOKUCHI, Norio, IRIE, Masachika
A major glucoamylase [EC 3.2.1.3] of Aspergillus saitoi was purified by ultra-filtration followed by successive chromatography on DEAE-Sephadex, Ultrogel AcA 44 and SP-Sephadex. The purification...
IWAHASHI, Kazuyuki, NAKAMURA, Kazuo (Torii), MITSUI, Yukio, OHGI, Kazuko, IRIE, Masachika
Binding of thymidine 3′,5′-diphosphate to ribonuclease was studied by spectroscopic, kinetic and crystallographic methods. The results show that the 5′-phosphate group is located close to the...
Carboxamidomethylation of a Ribonuclease from Aspergillus saitoi (1980)
The inactivation of a RNase from Aspergillus saitoi (RNase Ms) was studied to obtain information on its active site. Inactivation of RNase Ms by iodoacetamide was greater at an alkaline pH, and was...
Chemical Modification of Tryptophan Residues in Ribonuclease from a Rhizopus sp. (1980)
SANDA, Akihiro, IRIE, Masachika
Tryptophan residues in ribonuclease from a Rhizopus sp. (RNase Rh) were modified by NBS, H2O2-dioxane, o-nitrophenylsulfenyl chloride (NPS-Cl) and the relation between the extent of modification and...
Carboxymethylation of a Minor Ribonuclease from Aspergillus saitoi (1979)
RNase Ms was inactivated by iodoacetate. The inactivation was most rapid at pH 6.0, and was inhibited in the presence of a denaturant such as 8 M urea or 6 M guanidine-HCl. Competitive inhibitors...
WATANABE, Hideaki, OHGI, Kazuko, IRIE, Masachika
1. A base-nonspecific ribonuclease from Aspergillus saitoi [RNase Ms, EC 3.1.4.23; molecular weight, 12,500] was modified with phenyiglyoxal (PG) and I ,2-cyclohexanedione (CHD) in order to...
Studies on the binding of adenylyl-3', 5'-cytidine to ribonuclease (1978)
Torii, Kazuo, Urata, Yukihide, Iitaka, Yoichi, Mitsui, Yukio, Irie, Masachika
The interaction of adenylyl-3′, 5′-cytidine (ApC) with ribonuclease-S(RNase-S) was studied by X-ray difference Fourier synthesis at 4 Å resolution in parallel with kinetics and spectroscopic...
pH-Profiles of the Kinetic Parameters of a Minor Ribonuclease from Aspergillus saitoi (1978)
In order to investigate the nature of amino acid residues involved in the active site of a ribonuclease from Aspergillus saitoi, the pH-profiles of kinetic parameters of RNase Ms were measured. (1)...
The NBS oxidation of RNase M, which is base non-specific, was studied mainly by circular dichroism spectroscopy. It was found that tryptophan residues of RNase M were resistant to NBS at pH's from...
Photooxidation and Carbethoxylation of a Minor Ribonuclease from Aspergillus saitoi (1977)
IRIE, Masachika, OHGI, Kazuko, IWAMA, Masanori
In order to investigate the nature of amino acid residues involved in the active site of a ribonuclease from Aspergillus saitoi, the pH dependence of the rates of inactivation of RNase Ms by...
OHGI, Kazuko, KIRYU, Michiko, TORANO, Yumiyo, HORI, Yasuko, WATANABE, Hideaki, IWAMA, Masanori, ...
In order to investigate whether amino-groups are involved directly in the active site of RNase Ms, a minor ribonuclease from Asp. saitoi, trinitrophenylation of RNase Ms was investigated. At pH 7.7...
Further Studies on the Specificity of the Minor Ribonuclease from Aspergillus saitoi (1976)
In order to investigate the base specificity of the minor RNase [EC 3.1. 4. 23] from Aspergillus saitoi, the kinetic constant of the enzyme was measured with 16 dinucleoside phosphates (XpY's) as...
Studies on the State of Tyrosyl Residues in a Ribonuclease from Seminal Vesicles (1975)
In order to study the state of tyrosyl residues in a ribouuclease from bovine semina vesicles [EC 3. 1.4. 22, RNase Vs1] several lines of experiments were carried out. Spectrophotometric titration of...
Purification and Properties of a New Ribonuclease from Aspergillus saitoi (1975)
From a commercial digestive produced from Aspergillus saitoi, a ribonuclease [EC 3.1.4.23] having a molecular weight of 12,500 has been isolated in addition to the RNase reported previously, which...
Renaturation of Yeast Inorganic Pyrophosphatase Denatured in Urea and Guanidine Hydrochloride (1975)
YANO, Yoshiaki, IRIE, Masachika
The renaturation of yeast inorganic pyrophosphatase [EC 3.6.1.1] (PP1ase) denatured in guanidine-HCl and urea was studied. The molecular weight of PP1ase was estimated to be ca. 63,000–70,000 by...
The Inactivation of Ribonuclease from Seminal Vesicles by Photooxidation and Carbethoxylation (1974)
Carboxamidomethylation of Ribonuclease from Rhizopus sp. (1974)
KOMIYAMA, Tadazumi, IRIE, Masachika
1) A ribonuclease [EC 2. 7.7.17] from Rhizopus sp. (RNase Rh) was found to be in-activated by various halo-fatty acids and iodoacetamide. The inactivation of RNase Rh by iodoacetamide and...
Reoxidation of Reduced Ribonuclease from Bovine Seminal Vesicles (1974)
IRIE, Masachika, TSUBOTA, Akie
Ribonuclease [EC 3.1.4.22] from bovine seminal vesicles, having a molecular weight of 25,500, was reduced with 2-mercaptoethanol. The reduced RNase Vs1 was inactive enzymatically and its molecular...
Alkylation of Ribonuclease from Aspergillus saitoi with Iodoacetate and Iodoacetamide (1973)
HARADA, Masatomi, IRIE, Masachika
1) In order to obtain the knowledge on the active site of ribonuclease from Aspergillus saitoi (RNase M) [EC 2.7.7.17], chemical modifications of RNase M by various kinds of halo fatty acids and...
Carboxamidomethylation of Yeast Inorganic Pyrophosphatase (1973)
YANO, Yoshiaki, NEGI, Tahei, IRIE, Masachika
1) Yeast inorganic pyrophosphatase [EC 3.6.1.1, PPiase] was found to be inactivated by iodoacetamide. 2) The rate of inactivation of PP,ase by iodoacetamide was minimum at pH 7.0 in the range tested....
IRIE, Masachika, SUITO, Fumie, SAITO, Terumi
1) Amino acid composition and amino- and carboxyl-terminal amino acids of a ribonuclease (RNase Vs2) having molecular weight of 13, 000 from bovine seminal vesicles were determined. 2) Using antisera...
NEGI, Tahei, SAMEJIMA, Tatsuya, IRIE, Masachika
In order to investigate the role of tryptophan residues on the activity of inorganic pyrophosphatase [EC 3.6.1.1, PPiase], several lines of experiments were carried out. Methylenediphosphonate...
pH Profiles of the Kinetic Parameters and Photoinactivation of Ribonuclease from Rhizopus sp. (1972)
KOMIYAMA, Tadazumi, IRIE, Masachika
Ribonuclease from Rhizopus sp. (RNase Rh) [EC 2.7.7.17] was found to be inhibited competitively by various kinds of nucleotides. The inhibitory effect of the nucleotides having the phosphate group...
Studies on the State of Tryptophan Residues in Ribonuclease from Aspergillus saitoi (1972)
IRIE, Masachika, HARADA, Masatomi, SAWADA, Fumio
1) In order to investigate the roles of tryptophan residues in the active site of ribonuclease from Aspergillus saitoi [RNase M, EC 2. 7. 7. 17] several lines of experiments were carried out. 2)...
3-Acetoxy-l-acetyl-5-methylpyrazole, a Novel Acetylating Reagent of Protein (1972)
IRIE, Masachika, MIYASAKA, Tadashi, ARAKAWA, Kiichi
1. The reactivity of 3-acetoxy-l-acetyl-5-methylpyrazole (AAMP) with amino and hydroxyl groups of proteins has been studied. 2. AAMP was rather stable in an aqueous solution (pH 7.5) than...
IRIE, Masachika, HOSOKAWA, Shunji
(1) The rates of cleavage of dinucleoside phosphates (XpY) and of hydrolysis of nucleoside cyclic phosphates by RNases from bovine seminal vesicles (RNase Vs1 and Vs2) [EC 2. 7. 7.16] were measured...
Some Chemical and Physical Properties of Ribonuclease from Aspergillus saitoi (1971)
IRIE, Masachika, HARADA, Masatomi, NEGI, Tahei, SAMEJIMA, Tatsuya
1) The process for purification of ribonuclease [EC 2.7.7.17] (RNase M) from Aspergillus saitoi was improved. The yield was about twice that reported previously. The purified enzyme was homogeneous...
Purification and Properties of Seminal Vesicle Ribonucleases (1971)
HOSOKAWA, Shunji, IRIE, Masachika
1) Two ribonuclease [EC 2. 7. 7.16], RNases Vs1 and Vs2, were isolated from bovine seminal vesicles. They were purified 380 and 460 fold respectively, by CM-cellulose, Sephadex G-75 and P-cellulose...
Purification and Properties of a Ribonuclease from Rhizopus Species (1971)
KOMIYAMA, Tadazumi, IRIE, Masachika
1) The purification procedures of a ribonuclease [EC 2.7. 7.17] from Rhizopus sp. were revised. The yield of the crystalline enzyme was about 35%. The crystalline enzyme was shown to be...
1) In order to investigate the state of the tryptophan residue in RNase T1 [EC 2. 7. 7. 26] and carboxymethyl RNase T1 (CMRNase T1), fluorescence emission spectra of these enzymes were measured in...
Studies on the Photooxidation of Ribonuclease T1 (1970)
1. Photooxidation of ribonuclease T1(EC 2.7.7.26) was studied to obtain information on the active center of the enzyme. The effect of pH on the photo-inactivation rate indicated the involvement of a...
Inhibition of Ribonuclease from Aspergillus saitoi by Nucleosides (1969)
1.Ribonuclease from Aspergillus saitoi [RNase M, EC 2.7.7.17] was found to be inhibited competitively by various nucleosides. Among four common ribonucleosides, the inhibitory effect was in the...
pH-Profiles of the Kinetic Parameters of Ribonuclease from Aspergillus saitoi (1969)
1. Ribonuclease from Aspergillus saitoi [EC 2.7.7. 17] (RNase M) was found to be inhibited competitively by various kinds of nucleotides. The inhibitory effect of the nucleotides having the phosphate...
TAKAHASHI, TOMOKO, IRIE, MASACHIKA, UKITA, TYUNOSIN
The enzymatic activity of subtilisin-produced derivatives of ribonuclease A (RNase A) [EG 2. 7. 7. 16, ribonucleate pyrimidinenuclcotido2′-transferase (cyclizing)], ribonuclease S (RNase S) and...
1. Kinetic parameters, Km and Vmax, of several pancreatic ribonucleases [EC 2. 7.7.16], such as bovine, whale, porcine and horse RNases, were measured using nucleoside cyclic phosphates and...
Substrate Specificity of Ribonuclease from Aspergillus saitoi (1968)
IMAZAWA, MASAOKI, IRIE, MASACHIKA, UKITA, TYUNOSIN
1. The substrate specificity of Ribonuclease M [EC 2.7.7.17, Ribo-nucleate nucleotido-2'-transferase (cyclizing)], which was obtained from Aspergillus saitoi, was studied in detail using several...
A Kinetic Study on Ribonuclease T1 using Dinucleoside Phosphates as Substrates (1968)
1. Kinetic parameters, Km and Vmax, of RNase T1 [EC 2.7.7.26] were obtained usineg dinucleoside phosphate, GpX (GpA, GpC, GpG and GpU), as substrate at pH 7.5 and 5.0. Km values of four GpX's were...
Purification and Properties of Porcine Pancreatic Ribonuclease (1968)
YAMASAKI, YOSHIO, MURAKAMI, KEISUKE, IRIE, MASACHIKA, UKITA, YUNOSIN
1. A ribonuclease (RNase P) was isolated from porcine pancreas. The enzyme was purified by means of ammonium sulfate fractionation, phenol extraction, DEAE-, Phospho- and CM-cellulose column...
A Consideration on the Ultraviolet Spectrum of Ribonuclease A-Inhibitor Complex (1968)
1. A hypothesis which explains the difference spectrum between that of the RNase A [EC 2.7.7.16]-inhibitor complex and those of its constituents was proposed. This hypothesis is based on two...
Isolation and Properties of a Ribonuclease from Aspergillus saitoi (1967)
1.A ribonuclease, (RNase M) [EC 2.7.7.17 ribonucleate nucleotido-2’-transferase (cyclizing)] was isolated from “Molsin” (Aspergillus saitoi). RNase M was purified about 125 fold by means of...
Effect of Divalent Cations on Bovine Pancreatic Ribonucrease (1967)
TAKAHASHI, TOMOKO, IRIE, MASACHIKA, UKITA, TYUNOSIN
1. Effect of various divalent cations on Ribonuclease A [EC 2.7.7.16, ribonucleate pyrimidinenucleotido-2′transferase (cyclizing)] (RNase A) activity was reinvestigated with well-characterized...
pH-Profile of the Kinetic Parameters of Ribonuclease T1 (1967)
1. Kinetic parameters, Km and Vmax, of RNase T1 [EC 2.7.7.26] were obtained using G-cyclic-p as substrate at various pH's. From the pKm-, log Vmax-pH profile, two pKa's of free enzyme (pKe) and pKa...
Purification and Properties of Horse Pancreatic Ribonuclease (1967)
ISHIHARA, TATSUO, IRIE, MASACHIKA, UKITA, TYNOSIN
1. Two ribonucleases [EG 2.7.7.16], RNase Eq1 and Eq2,were purified 180 and 130 fold, respectively, by successive IRG-50 and phos-phocellulose column chromatography after ammonium sulfate...
Purification and Characterization of Caffeine Synthase from Tea Leaves1
Kato, Misako, Mizuno, Kouichi, Fujimura, Tatsuhito, Iwama, Masanori, Irie, Masachika, Crozier, Alan, ...
Caffeine synthase (CS), the S-adenosylmethionine-dependent N-methyltransferase involved in the last two steps of caffeine biosynthesis, was extracted from young tea (Camellia sinensis) leaves; the CS...
Purification and Characterization of Caffeine Synthase from Tea Leaves1
Kato, Misako, Mizuno, Kouichi, Fujimura, Tatsuhito, Iwama, Masanori, Irie, Masachika, Crozier, Alan, ...
Caffeine synthase (CS), the S-adenosylmethionine-dependent N-methyltransferase involved in the last two steps of caffeine biosynthesis, was extracted from young tea (Camellia sinensis) leaves; the CS...