The purification of hypertensin I has been described. The final product which is four times as powerful a pressor agent as l-arterenol, is obtained with an over-all recovery of 40 per cent. The product consists of a single component in countercurrent distribution, having a nitrogen content of 15.97 per cent and a specific activity of 7050 Goldblatt units per mg. of N or 1125 units per mg. of solid. Acid hydrolysis and paper chromatography indicate in a preliminary fashion that there are about nine amino acids present in the intact polypeptide.
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http://dx.doi.org/10.1084/jem.100.4.363 | DOI Listing |
J Cardiovasc Med (Hagerstown)
April 2010
Instituto de Investigaciones Cardiológicas Prof. Dr Alberto C. Taquini, Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas, Buenos Aires, Argentina.
In 1939, two independent teams, in Buenos Aires and Indianapolis, identified the polypeptide angiotensin. In 1934, Goldblatt et al. demonstrated that partial occlusion of the renal arteries produces hypertension in dogs, and Houssay in 1936 predicted the presence of a humoral mechanism and, with Fasciolo, demonstrated that the ischemic kidneys released a pressor substance that increased the recipient's blood pressure.
View Article and Find Full Text PDFElectrophoresis
April 2008
Department of Chemistry, National Taiwan University, Taipei, Taiwan.
A macrocyclic polyamine, 1,5,9,13,17,21,25,29-octaazacyclodotriacontane ([32]ane-N(8)), in the bonded phase was employed as a molecular receptor for CEC separation of oligopeptides. Parameters affecting the performance of the separations were considered. Baseline separation for the mixture of angiotensin I, angiotensin II, [Sar(1), Thr(8)]-angiotensin II, beta-casomorphin bovine, beta-casomorphin human, oxytocin acetate, tocinoic acid, vasopressin, and FMRF amide could be achieved using phosphate buffer (30 mM, pH 7) as the mobile phase.
View Article and Find Full Text PDFJ Biochem
April 1998
Department of Physiological Chemistry and Metabolism, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033.
A chymotrypsin-like proteinase, designated myonase, was successfully purified to homogeneity from X-chromosome linked muscular dystrophic mouse skeletal muscle by affinity chromatography on agarose conjugated with lima bean trypsin inhibitor as ligand. The molecular mass of the purified myonase was determined to be 26 kDa by SDS-PAGE and to be 25,187 Da by mass spectrometry. The native enzyme is a single chain molecule and a monomeric protein without sugar side-chains.
View Article and Find Full Text PDFBiol Pharm Bull
August 1997
Department of Pharmaceutics, Gifu Pharmaceutical University, Japan.
Carboxylesterases (EC 3.1.1.
View Article and Find Full Text PDFBiol Pharm Bull
January 1997
Department of Pharmaceutics, Gifu Pharmaceutical University, Japan.
Two carboxylesterases with pI 6.0 and 6.2 derived from rat liver microsomes were purified.
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