𝔖 Bobbio Scriptorium
✦   LIBER   ✦

A unique activity assay for carboxypeptidase A in human serum

✍ Scribed by Lynn M. Peterson; Barton Holmquist; J.L. Bethune


Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
624 KB
Volume
125
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis


Measurement of carboxypeptidase A, one of the pancreatic proteolytic enzymes, in human serum is made possible by a combination of affinity chromatography to isolate and concentrate the enzyme followed by monitoring activity spectrophotometrically with a high-turnover pep tide substrate. Concentrations of enzyme in the nanogram-per-milliliter range can be determined with high precision and reliability. Initial clinical application of this method demonstrates no detectable activity in serum from normal individuals, but the enzyme is present in the sera of individuals with pancreatitis.


πŸ“œ SIMILAR VOLUMES


Flow cytometric assay for estimating fun
✍ Edith Martin; Ute Schlasius; Sucharit Bhakdi πŸ“‚ Article πŸ“… 1992 πŸ› Springer-Verlag 🌐 English βš– 615 KB

We describe a simple and rapid bioassay for estimating fungicidal activity of Amphotericin B in human serum using flow cytometry. The method exploits the fact that Candida albicans damaged by Amphotericin B show a decrease in size and take up propidium iodide to exhibit a red fluorescence after deox

A direct spectrophotometric assay for d-
✍ R.F. Pratt; W.Stephen Faraci; Chandrika P. Govardhan πŸ“‚ Article πŸ“… 1985 πŸ› Elsevier Science 🌐 English βš– 258 KB

A direct spectrophotometric pH indicator method has been devised to assay the activity of the D-Ala carboxypeptidase/transpeptidase of Streptomyces R61, and which should be of general application to D-Ala carboxypeptidases. The substrate employed is N,N'diacetyl-r.lysyl-D-alanyl-D-lactate. The metho

A rapid fluorometric assay for the deter
✍ M. Merchant; J. Small; R. Falconi; B.J. Crookshank πŸ“‚ Article πŸ“… 2009 πŸ› Elsevier Science 🌐 English βš– 241 KB

Phospholipase A 2 (PLA 2 ) is an enzyme that cleaves fatty acids from the sn-2 position of membrane phospholipids. Intracellular PLA 2 has been shown to be important for the generation of arachidonic acid, which leads to the synthesis of a wide range of eicosanoid paracrine hormones. Furthermore, se