The amino acid composition of hypertensin II and its biochemical relationship to hypertensin I
KE Lentz, LT Skeggs Jr, KR Woods, JR Kahn… - The Journal of …, 1956 - rupress.org
KE Lentz, LT Skeggs Jr, KR Woods, JR Kahn, NP Shumway
The Journal of Experimental Medicine, 1956•rupress.orgPreparations 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,
were quantitatively analyzed for their amino acid content. Chromatography on ion exchange
columns showed the presence of equimolar amounts of aspartic acid, proline, valine,
isoleucine, tyrosine, phenylalanine, histidine, and arginine. Hypertensin I was found to
contain one mole of leucine and one mole of histidine in addition to the amino acids of …
the hypertensin converting enzyme of plasma and purified by countercurrent distribution,
were quantitatively analyzed for their amino acid content. Chromatography on ion exchange
columns showed the presence of equimolar amounts of aspartic acid, proline, valine,
isoleucine, tyrosine, phenylalanine, histidine, and arginine. Hypertensin I was found to
contain one mole of leucine and one mole of histidine in addition to the amino acids of …
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, were quantitatively analyzed for their amino acid content. Chromatography on ion exchange columns showed the presence of equimolar amounts of aspartic acid, proline, valine, isoleucine, tyrosine, phenylalanine, histidine, and arginine.
Hypertensin I was found to contain one mole of leucine and one mole of histidine in addition to the amino acids of hypertensin II. These two amino acids were isolated from the conversion products of hypertensin I and identified as the peptide histidylleucine.
Carboxypeptidase digestion of hypertensin I showed the carboxyl terminal sequence of amino acids to be residue-phenylalanyl-histidylleucine. Similar studies of hypertensin II demonstrated residue-phenylalanine. It was concluded that the conversion of hypertensin I by the plasma hypertensin converting enzyme involved hydrolysis of the phenylalanyl-histidine bond to form hypertensin II and histidylleucine. The further removal by carboxypeptidase of phenylalanine from hypertensin II destroyed all of the vasoconstrictor activity.
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