منابع مشابه
Enzymatic hydrolysis of steroid hormone esters by blood serum.
In recent years the concept of the specificity of enzyme action has been subjected to revision. The proteolytic enzymes (1) have been shown to have esterase activity and the concept of a blood esterase as distinct from a blood lipase is no longer tenable (2). The enzymatic hydrolysis of the steroid hormone esters by blood sera (3) had not been suspected until solubility determinations of the es...
متن کاملMetabolism of glutathione. II. Determination of glutathione and products of its hydrolysis in blood.
A method for the determination of glutathione and the sulfur-containing products of the hydrolysis of glutathione has been developed in this laboratory. This method has been applied to tissues, enzymatic digests, and blood. This report is concerned with the description of the method for blood. The method depends upon (1) the lability of the y-glutamyl linkage to mild hydrolysis with acid and (2...
متن کاملEnzymatic oxidation and hydrolysis of glutathione by different tissues.
The enzymatic oxidation of reduced glutathione through a cytochrome c-linked system by a cell-free preparation of mouse kidney has been reported previously (1). Neubeck and Smythe (2) have reported the use of guinea pig liver to hydrolyze glutathione enzymatically with the liberation of cysteine; this system has been reviewed recently by Smythe (3). In this contribution the relative rates of en...
متن کاملThe Oxidation of Glutathione by Serum.
Studies of serum glutathione reductase activity in thislaboratory prompted an attempt to demonstrate glutathione oxidase in the serum. The oxidation of reduced glutathione in the sera of patients with various diseases does not differ from normal sera. Preheating the serum and addition of cytochrome c does not effect the oxidizing capacity of the serum. The ability of serum to oxidize reduced gl...
متن کاملSubstance P hydrolysis by human serum cholinesterase.
Highly purified human serum cholinesterase (EC 3.1.1.8, also known as pseudocholinesterase and butyrylcholinesterase) had peptidase activity toward substance P. Digestion of substance P was monitored by high performance liquid chromatography, which separated three product peptides. The cleavages occurred sequentially. The first peptide to appear as Arg1-Pro2. The Km for this hydrolysis was 0.3 ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1939
ISSN: 0006-2936
DOI: 10.1042/bj0331171b