Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Yoshifumi Watazu"'
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 64:1352-1358
Mass production of an r-CDH derived from Nocardia species was made possible by gene technology. (Horinouchi et al., Applied and Environmental Microbiology, 57, 1386-1393 (1991)). However, the characteristics of the r-CDH have not been studied in deta
Autor:
Hiroaki Okabe, Nobuaki Kaneda, Sawao Murao, Yoshifumi Watazu, Katashi Nagamatsu, Yasushi Shirahase
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 58:745-751
A selective inactivating enzyme for the m-subunit of lactate dehydrogenase (LDH) was found in the culture filtrate of Penicillium citrinum KE-1, newly isolated from soil. The enzyme was purified from the culture filtrate by ammonium sulfate fractiona
Autor:
Yasushi Shirahase, Arthur Karmen, Nobuaki Kaneda, Hiroaki Okabe, Yoshifumi Watazu, Yoshinori Uji
Publikováno v:
Journal of Clinical Laboratory Analysis. 7:81-85
We studied a new proteinase K assay method for human serum mitochondrial aspartate aminotransferase. We found that proteinase K showed no inactivation of human mitochondrial aspartate aminotransferase isoenzyme and complete inactivation of cytosolic
Publikováno v:
Clinical Chemistry. 38:2193-2196
We devised a method for assaying serum lactate dehydrogenase isoenzyme 1 (LD-1) activity specifically by preincubation with alpha-chymotrypsin and guanidine. Cleavage of phenylalanine bonds in the loop of A and B subunits of LD-3, LD-4, and LD-5 isoe
Publikováno v:
Analytical Sciences. 7:333-335
Publikováno v:
Clinical Chemistry. 36:687-689
Total mitochondrial aspartate aminotransferase (EC 2.6.1.1), the sum of apo- and holo-mitochondrial aspartate aminotransferase activity in human serum, was measured by using a proteolytic method: inactivation of cytosolic aspartate aminotransferase w
Autor:
Nobuaki Kaneda, Yasushi Shirahase, Hiroyuki Sugiuchi, Yoshinori Uji, Yoshifumi Watazu, Hiroaki Okabe
Publikováno v:
Clinical biochemistry. 23(2)
A new proteolytic measurement of serum mitochondrial aspartate aminotransferase was evaluated using cytosolic aspartate aminotransferase inactivating protease. Some of the proteases, such as, alpha-chymotrypsin, subtilisin and cytosolic aspartate ami