Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr).

Literature DB >> 6347189

Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr).

G D McIntyre, B Leckie, A Hallett, M Szelke.

Abstract

A new affinity column for renin was prepared by coupling the isosteric peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr, where R is a reduced isosteric bond, -CH2-NH-), to activated 6-aminohexanoic acid-Sepharose 4B. Chromatography of a crude extract of human kidney cortex on this material resulted in a 5500-fold purification of renin in 76% yield. The purified enzyme (specific activity 871 units/mg) was free of non-specific acid-proteinase activity and was stable at pH 6.8 and -20 degrees C over a period of several weeks.

Entities: Chemical Gene Species

Mesh：

Substances：

Year: 1983 PMID： 6347189 PMCID： PMC1154389 DOI： 10.1042/bj2110519

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

15 in total

Review 1. Isoelectric points and molecular weights of proteins.

Authors: P G Righetti; T Caravaggio
Journal: J Chromatogr Date: 1976-04-21

2. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors: M M Bradford
Journal: Anal Biochem Date: 1976-05-07 Impact factor: 3.365

Purification of human renin by affinity chromatography using a new peptide inhibitor of renin, H.77 (D-His-Pro-Phe-His-LeuR-Leu-Val-Tyr).

Review 1. Isoelectric points and molecular weights of proteins.

2. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

3. Fluorometric assay of proteins in the nanogram range.

4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

5. Microassay for cathepsin D shows an unexpected effedt of cycloheximide on limb-bone rudiments in organ culture.

6. Silver staining of proteins in polyacrylamide gels.

7. Multiple forms of human renin. Purification and characterization.

8. A microassay for active and total renin concentration in human plasma based on antibody trapping.

9. Purification of pig renin.

10. Regulation of vitamin K-dependent carboxylation.

1. Similarity between physicochemical properties of recombinant rat prorenin and native inactive renin.

2. Identification of an enzyme in human kidney that correctly processes prorenin.

3. Affinity separation. Patents and literature.

4. A comparative study of the glomerular peripolar cell and the renin-secreting cell in twelve mammalian species.

5. The rapid purification and partial characterization of human serum angiotensinogen.

6. RPEL proteins are the molecular targets for CCG-1423, an inhibitor of Rho signaling.