Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Alain L. Marie"'
Publikováno v:
Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 359:857-862
M. luteus catalase dissociates upon treatment with urea, dodecylsulfate and anhydrides into monomers, the molecular weight of which appears to be 1/4 of that of the native enzyme. The urea-induced dissociation depends upon the incubation time, the ur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df7aba1e8c572d4acdd5c8616ef6e5ff
https://doi.org/10.1515/bchm2.1978.359.2.857
https://doi.org/10.1515/bchm2.1978.359.2.857
Autor:
Alain L. Marie
Publikováno v:
Canadian journal of biochemistry. 54(8)
Pyridoxal 5′-phosphate (PLP) in aqueous solutions can form a Schiff base complex with 14 and 16 lysine residues of rabbit and sturgeon muscle aldolases (EC 4.1.2.13), respectively. Although the mechanism of their interaction with PLP should be the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee9bc34c21c956599ffaa7bc3306de17
https://pubmed.ncbi.nlm.nih.gov/953852
https://pubmed.ncbi.nlm.nih.gov/953852
Publikováno v:
Journal of Molecular Biology. 129:675-676
Octahedral shaped crystals of about 1 mm were grown from catalase of Micrococcus luteus. The space group was determined as P422121 with a = b = 106.6 A and c = 106.3 A . In contrast to mammalian catalase, the bacterial catalase contains only one subu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c399e95695f4ff159348e218a9493606
https://doi.org/10.1016/0022-2836(79)90476-5
https://doi.org/10.1016/0022-2836(79)90476-5