Human plasma and serum trypsin-like esterase activity.
نویسنده
چکیده
A spectrophotometric method using benzoyl arginine ethyl ester (BAEE) is described for the assay of serum and plasma trypsin-like esterase activity. The method was used to find activities in serum and plasma (anticoagulated with oxalate and heparin) from 12 healthy males at 3 different reaction pH’s. The effects of calcium, oxalate, heparin, soybean trypsin inhibitor, ovomucoid, and heat on this activity were also measured. Values of esterase activity were significantly different, indicating a variable enzyme or inhibitor composition in the 3 sets of samples. Plasma from heparinized blood gave unique activity responses to pH and to the agents tested for effect.
منابع مشابه
Differentiation of trypsin-like enzymes in human plasma.
The arginine amidase and arginine esterase activity of human plasma is compared with that of trypsin, thrombin, plasmin, and kallikrein by using the homologous synthetic amino acid substrates, benzoyl arginine amide (BAA) and benzoyl arginine ethyl ester (BAEE). Hydrolyses of BAA and BAEE in plasma are distinguished by several features: pH optimum, heat stability, storage stability, effect of d...
متن کاملHuman plasma carboxyl esterase-catalyzed triolein hydrolysis. Existence of promoting factor in serum.
The possibility that some factor in serum changes the substrate specificity of purified human plasma carboxyl esterase, which hydrolyzes the short chain fatty acid ester, tributyrin, was investigated. The purified carboxyl esterase from human plasma hydrolyzed 48 mmol of tributyrin/mg of protein/h, monoolein at 1560 mumol of released fatty acids/mg of protein/h, diolein at 133 mumol of released...
متن کاملPartial purification of a serum inhibitor of C'1-esterase.
The first component of human complement (C’l) has been reported to exist in serum as a proenzyme which can be activated by antigen-antibody aggregates (l-5), plasmin (1, B), and, in a partially purified state, by autocatalysis (6, 7) to an enzyme, C’l-e&erase, capable of hydrolyzing certain synthetic amino acid esters, notably N-acetyl-L-tyrosine ethyl ester (6-8), and interacting with the four...
متن کاملDefective Esterase and Kinin-Forming Activity in Human Fletcher Trait Plasma A FRACTION RICH IN KALLIKREINLIKE ACTIVITY By Virginia
Fletcher trait plasma failed to generate kinin and developed only a small amount of arginine esterase activity at an abnormally slow rate following surface activation. Neither defect was due to a deficiency of Hageman factor (HF, factor XII) or kininogen or to an excessively rapid inactivation of evolving kinin. Pyrex pretreated with Fletcher trait plasma did not generate kinin normally in fres...
متن کاملDefective esterase and kinin-forming activity in human Fletcher trait plasma. A fraction rich in kallikreinlike activity.
Fletcher trait plasma failed to generate kinin and developed only a small amount of arginine esterase activity at an abnormally slow rate following surface activation. Neither defect was due to a deficiency of Hageman factor (HF, factor XII) or kininogen or to an excessively rapid inactivation of evolving kinin. Pyrex pretreated with Fletcher trait plasma did not generate kinin normally in fres...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Clinical chemistry
دوره 12 6 شماره
صفحات -
تاریخ انتشار 1966