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THE PREPARATION, PURIFICATION, AND AMINO ACID SEQUENCE OF A POLYPEPTIDE RENIN SUBSTRATE
A purified preparation of a polypeptide renin substrate prepared by tryptic degradation of the protein renin substrate has been analyzed by the fluorodinitrobenzene method and after degradation withExpand
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The biochemistry of the renin-angiotensin system.
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Hydrolysis of Bradykinin by Angiotensin‐Converting Enzyme
Two dipeptides, phenylalanylarginine (Phe-Arg) and serylproline (Ser-Pro), are released sequentially from bradykinin by angiotensin-converting enzyme purified from hog lungs; chloride increases theExpand
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The biochemistry of the renin-angiotensin system and its role in hypertension.
The renin-angiotensin system has an important role in maintaining elevated blood pressure levels in certain forms of experimental and human hypertension. Renin, an enzyme produced by theExpand
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Pseudorenin. A new angiotensin-forming enzyme.
A new enzyme, pseudorenin, has been discovered which resembles renin in its ability to form angiotensin I from the synthetic tetradecapeptide renin substrate and from purified hog renin substrate A.Expand
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THE AMINO ACID COMPOSITION OF HYPERTENSIN II AND ITS BIOCHEMICAL RELATIONSHIP TO HYPERTENSIN I
Preparations of hypertensin II, obtained from the treatment of hypertensin I by the action of the hypertensin converting enzyme of plasma and purified by countercurrent distribution, wereExpand
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THE SYNTHESIS OF A TETRADECAPEPTIDE RENIN SUBSTRATE
A tetradecapeptide renin substrate having a biological activity comparable to the natural product and similar chemical properties has been synthesized by means of the carbobenzyloxyl azide and mixedExpand
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KINETICS OF THE REACTION OF RENIN WITH NINE SYNTHETIC PEPTIDE SUBSTRATES
A number of peptides have been synthesized which represent portions of the tetradecapeptide renin substrate molecule, and which contain the hydrolyzable leu-leu bond. An automatic chemical method forExpand
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THE AMINO ACID SEQUENCE OF HYPERTENSIN II
The amino acid sequence of horse hypertensin II has been determined by the use of chymotrypsin, the fluorodinitrobenzene method, and stepwise phenylisothiocyanate degradation. The results indicateExpand
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A comparison of the substrate specificities of cathepsin D and pseudorenin.
Cathepsin D, purified from hog spleen, releases angiotensin I from tetradecapeptide renin substrate and from protein renin substrates purified from hog and human plasma. However, the enzyme does notExpand
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