Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Jun'ichi Hase"'
Autor:
Tsuneo Takadera, Ken'ichiro Mitsui, Jun'ichi Hase, Kazushi Iwata, Kyoichi Kobashi, Noboru Nakai
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 611:205-213
Carp muscle alkaline protease consists of four kinds of subunits, and its composition was assumed to be (αβγ2δ2)4. It dissociated in the presence of 2-mercaptoethanol into an enzyme and α-subunits which upon removal of 2-mercaptoethanol rapidly
Publikováno v:
The Journal of Biochemistry. 95:535-541
Jack bean urease [EC 3.5.1.5] was modified with diazonium-1H-tetrazole (DHT). Reaction of DHT with the enzyme produced a characteristic absorption peak at 320 nm and led to complete loss of the enzymatic activity at a low concentration of DHT. Amino
Publikováno v:
NIPPON SUISAN GAKKAISHI. 40:201-209
Publikováno v:
Biochemical and Biophysical Research Communications. 83:881-885
Rabbit muscle aldolase is inactivated by cathepsin B1 to approximately 10 percent of the original activity for fructose-1, 6-bisphosphate cleavage without change in the fructose-1-phosphate cleavage activity. Activity loss is related to release of on
Publikováno v:
Journal of Pharmacobio-Dynamics. 6:61-70
The electronic structures of 34 hydroxamic acids [R-(CONHCH2(n-CONHOH, R = aromatic or aliphatic, n = 1 or 0] were calculated by the INDO method and their urease inhibitory potencies were discussed in terms of the calculated electronic parameters and
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 558:307-313
Perfringolysin O revealed ring- and arc-shaped structures in the absence of cholesterol by negative staining electron microscopy, while before activation with cysteine it showed indistinct arcs and irregularly curved sticks but no rings. These struct
Publikováno v:
NIPPON SUISAN GAKKAISHI. 45:157-161
Publikováno v:
Journal of Pharmacobio-Dynamics. 3:457-462
Quantitative structure activity relationships between physico-chemical properties of four series of more than sixty hydroxamic acids [R-(CONHCH2)n-CONHOH, R=aromatic or aliphatic, n=1 or 0) and their urease inhibitory activities were examined. The be
Publikováno v:
NIPPON SUISAN GAKKAISHI. 43:307-314
Some enzymatic properties of the highly purifted cathepsin A from white muscle of carp were examined. The optimal pH of the cathepsin A was 4.6 in 0.2M acetate buffer solution. Approximate Km values of the cathepsin A for carbobenzoxy (CBZ)-Glu-Phe,
Publikováno v:
NIPPON SUISAN GAKKAISHI. 43:181-193