HYDROLYSIS OF MERCURIPAPAIN BY LEUCINE AMINOPEPTIDASE WITHOUT LOSS OF ENZYMIC ACTIVITY
نویسندگان
چکیده
منابع مشابه
The specificity of leucine aminopeptidase.
Since Linderstr@m-Lang’s demonstration that the hydrolysis of Lleucylglycine (LG) is due to a distinctileucyl peptidase (l), various studies have shown that this enzyme is widely distributed (24) and requires for its activity the presence of Mn++ or Mg++ ions (2, 5). The enzyme has been regarded as a typical aminopeptidase (5), since it does not hydrolyze acylated compounds Such as benzoyl-L-le...
متن کاملLeucine Aminopeptidase (Bovine Lens)
The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...
متن کاملLocalization of Leucine Aminopeptidase Isoenzymes.
A simple, sensitive staining procedure for the localization of leucine aminopeptidase isoenzymes after electrophoretic separation on cellulose acetate membranes is described. Separation of leucine aminopeptidase isoenzymes, using cellulose acetate membranes, does not appear to be a rewarding diagnostic procedure in the investigation of hepatobiliary or pancreatic disorders.
متن کاملThe enzymic hydrolysis of carrageenin.
Carrageenin is the water soluble polysaccharide extractable from the red algae Chondrus crispus and Gigartina stellata. The polysaccharide is essentially a polymer of alpha-D-galactopyranoside-4-sulphate. Smith et al. (1954) fractionated carrageenin with potassium chloride into two components and obtained a precipitable component which could form gels and a nongelling component which remained i...
متن کاملLeucine Aminopeptidase (Bovine Lens)
Spark emission and atomic absorption spectroscopy of crystalline leucine aminopeptidase (bovine lens) (EC 3.4.1.1) shows the presence of 2 zinc atoms per subunit molecular weight of 54,000 (12 zinc atoms per oligomer of 320,000). Removal of zinc by dialysis yields a zinc-free product with no enzymatic activity which upon readdition of Zn2+, regains full activity with the concomitant binding of ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1958
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)77291-3