Radioimmunoassay of pig pancreatic elastase

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Development of a radioimmunoassay for pig pancreatic kallikrein.

A radioimmunoassay for the determination of pig pancreatic kallikrein was developed. The chloramine-T method was employed for the labelling of the antigen with 125I. The assay allows the determination of kallikrein in concentrations as low as 0.4 microgram/l. Pig urinary and pig submandibular kallikreins are indistinguishable from pig pancreatic kallikrein by the assay. No cross reactivity was ...

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Isolation and characterization of a pancreatic elastase

1. An elastase-like enzyme in plasma of patients with acute pancreatitis was purified by DEAE-cellulose column chromatography and polyacrylamide-gel disc electrophoresis. 2. In this way 0.24 mg of purified enzyme with a specific activity of 3-94 succinyl-L-alanylL-alanyl-L-alanyl-p-nitroanilide units/mg of protein was obtained from 10 ml of plasma. 3. The purified material was homogeneous as as...

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The specificity of purified porcine pancreatic elastase.

An electrophoretically homogeneous elastase preparation free from tryptic and chymotryptic activities was obtained by chromatography on DEAE-Sephadex and CM-cellulose. This preparation exhibits a narrower specificity towards peptide bonds than that observed by Naughton & Sanger (1961). With oxidized insulin B chain as substrate, the fastest breaks occur between alanine-14 and leucine-15 and bet...

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Pancreatic elastase: purification, properties, and function.

The enzyme elastase, characterized by its ability to dissolve elastin, has been studied in recent years by Ba16 and Banga (1). These investigators described its occurrence in pancreas, an assay for its determination, and work on its purification. Crystallization of the enzyme from beef pancreas has been reported by Banga (2), although no studies on homogeneity or properties of the crystalline m...

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Pig pancreatic anhydro-elastase. Role of the serine-195 hydroxy group in the binding of inhibitors and substrate.

The binding constants of a number of ligands were measured for pancreatic elastase (PE) and anhydro-elastase (AE) in order to assess the contribution of Ser-195 to substrate and inhibitor binding by PE. AE was purified by affinity chromatography on a column containing immobilized turkey ovomucoid inhibitor. The AE had 0.1 +/- 0.1% of the activity of the native enzyme and contained 0.8 +/- 0.06 ...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1977

ISSN: 0014-5793

DOI: 10.1016/0014-5793(77)80193-2