The isolation of a hypertensin
- 1 March 1956
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 62 (3), 520-527
- https://doi.org/10.1042/bj0620520
Abstract
Hypertensin formed by the action of rabbit renin on ox serum was resolved by partition chromatography into 3 active components. The amphoteric nature of the major active component was shown by electrophoresis on paper. The major active component was isolated in a form which appears to be homogeneous It is a peptide containing 8 different amino acids which are present as 10 residues in its mimimum stoichiometric unit. It shows a pressor action up to 3 times that of (-) nor-epinephrine. The hypertensin isolated in this work was compared with hypertensins previously described.Keywords
This publication has 13 references indexed in Scilit:
- The purification of hypertensin.1955
- A new method of large-scale preparation of hypertensin, with a note on its assayBiochemical Journal, 1955
- Purification of Angiotonin (Hypertensin)Science, 1955
- THE PURIFICATION OF HYPERTENSIN IThe Journal of Experimental Medicine, 1954
- THE EXISTENCE OF TWO FORMS OF HYPERTENSINThe Journal of Experimental Medicine, 1954
- The amino-acid sequence in the glycyl chain of insulin. 1. The identification of lower peptides from partial hydrolysatesBiochemical Journal, 1953
- THE ISOLATION AND ASSAY OF HYPERTENSIN FROM BLOODThe Journal of Experimental Medicine, 1952
- Ultraviolet Absorption Spectra of Proteins and Amino AcidsAdvances in protein chemistry, 1952
- Quantitative Microdetermination of Amino Acids after Paper ChromatographyScience, 1951
- The separation of N-2:4-dinitrophenyl amino-acids on paper chromatogramsBiochemical Journal, 1951