The preparation, purification, and amino acid sequence of a polypeptide renin substrate
LT Skeggs Jr, JR Kahn, K Lentz… - The Journal of …, 1957 - rupress.org
LT Skeggs Jr, JR Kahn, K Lentz, NP Shumway
The Journal of experimental medicine, 1957•rupress.orgA 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 with renin, carboxypeptidase, and phenylisothiocyanate, has been found to
possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser.
The first 10 of these amino acids constitutes hypertensin I which is released by cleavage of
the leucyl-leucine bond by renin. The remaining 4 amino acids, leu, val, tyr, ser, apparently …
protein renin substrate has been analyzed by the fluorodinitrobenzene method and after
degradation with renin, carboxypeptidase, and phenylisothiocyanate, has been found to
possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser.
The first 10 of these amino acids constitutes hypertensin I which is released by cleavage of
the leucyl-leucine bond by renin. The remaining 4 amino acids, leu, val, tyr, ser, apparently …
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 with renin, carboxypeptidase, and phenylisothiocyanate, has been found to possess the amino acid sequence; asp-arg-val-tyr-ileu-his-pro-phe-his-leu-leu-val-tyr-ser. The first 10 of these amino acids constitutes hypertensin I which is released by cleavage of the leucyl-leucine bond by renin. The remaining 4 amino acids, leu, val, tyr, ser, apparently link hypertensin I to the protein renin substrate.
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