Further studies on the enzymatic and chemical inactivation of hypothalamic FSH-RH

Andrew V. Schally; Yoshihiko Baba; Tommie W. Redding; Hisayuki Matsuo; Akira Arimura

doi:10.1159/000122022

Further studies on the enzymatic and chemical inactivation of hypothalamic FSH-RH

Andrew V. Schally, Yoshihiko Baba, Tommie W. Redding, Hisayuki Matsuo, Akira Arimura

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

The cffect of chemical and enzymatic treatments on the biological activity of porcine follicle-stimulating hormone- releasing hormone (FSH-RH) was studied. FSH-RH activity was not affected by trypsin, pepsin, neuraminidase, carboxy- peptidasc A, aminopeptidase M and leucine aminopcptidase. However, incubation with chymotrypsin, subtilisin, papain and pyrrolidonc carboxylyl peptidase abolished the FSH-RI1 activity as did treatment with hydrochloric acid (0.9 m, 1 h, 100°C), diazotized sulfanilic acid, and N-bromosuccinimide. Nitrous acid, sodium mctaperiodate, and ninhydrin did not affect the FSH-RII activity appreciably. Amino acid analyses of the purest FSH-RH preparation showed the following composition: His 1, Arg 1, Scr 1, Glu 1, Pro 1, Gly 2, Leu 1, Trp 1, and Tyr 1. These results and information obtained during purification procedures indicate that a basic polypeptide composed of ten amino acids possesses both LIl-RH and FSII-RH activity.

Original language	English (US)
Pages (from-to)	347-358
Number of pages	12
Journal	Neuroendocrinology
Volume	8
Issue number	6
DOIs	https://doi.org/10.1159/000122022
State	Published - Jan 1 1971
Externally published	Yes

Keywords

FSH-relcasing hormone
LH-releasing hormone
Polypeptide

ASJC Scopus subject areas

Endocrinology, Diabetes and Metabolism
Endocrinology
Endocrine and Autonomic Systems
Cellular and Molecular Neuroscience

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10.1159/000122022

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title = "Further studies on the enzymatic and chemical inactivation of hypothalamic FSH-RH",

abstract = "The cffect of chemical and enzymatic treatments on the biological activity of porcine follicle-stimulating hormone- releasing hormone (FSH-RH) was studied. FSH-RH activity was not affected by trypsin, pepsin, neuraminidase, carboxy- peptidasc A, aminopeptidase M and leucine aminopcptidase. However, incubation with chymotrypsin, subtilisin, papain and pyrrolidonc carboxylyl peptidase abolished the FSH-RI1 activity as did treatment with hydrochloric acid (0.9 m, 1 h, 100°C), diazotized sulfanilic acid, and N-bromosuccinimide. Nitrous acid, sodium mctaperiodate, and ninhydrin did not affect the FSH-RII activity appreciably. Amino acid analyses of the purest FSH-RH preparation showed the following composition: His 1, Arg 1, Scr 1, Glu 1, Pro 1, Gly 2, Leu 1, Trp 1, and Tyr 1. These results and information obtained during purification procedures indicate that a basic polypeptide composed of ten amino acids possesses both LIl-RH and FSII-RH activity.",

keywords = "FSH-relcasing hormone, LH-releasing hormone, Polypeptide",

author = "Schally, {Andrew V.} and Yoshihiko Baba and Redding, {Tommie W.} and Hisayuki Matsuo and Akira Arimura",

year = "1971",

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doi = "10.1159/000122022",

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AU - Schally, Andrew V.

AU - Baba, Yoshihiko

AU - Redding, Tommie W.

AU - Matsuo, Hisayuki

AU - Arimura, Akira

PY - 1971/1/1

Y1 - 1971/1/1

N2 - The cffect of chemical and enzymatic treatments on the biological activity of porcine follicle-stimulating hormone- releasing hormone (FSH-RH) was studied. FSH-RH activity was not affected by trypsin, pepsin, neuraminidase, carboxy- peptidasc A, aminopeptidase M and leucine aminopcptidase. However, incubation with chymotrypsin, subtilisin, papain and pyrrolidonc carboxylyl peptidase abolished the FSH-RI1 activity as did treatment with hydrochloric acid (0.9 m, 1 h, 100°C), diazotized sulfanilic acid, and N-bromosuccinimide. Nitrous acid, sodium mctaperiodate, and ninhydrin did not affect the FSH-RII activity appreciably. Amino acid analyses of the purest FSH-RH preparation showed the following composition: His 1, Arg 1, Scr 1, Glu 1, Pro 1, Gly 2, Leu 1, Trp 1, and Tyr 1. These results and information obtained during purification procedures indicate that a basic polypeptide composed of ten amino acids possesses both LIl-RH and FSII-RH activity.

AB - The cffect of chemical and enzymatic treatments on the biological activity of porcine follicle-stimulating hormone- releasing hormone (FSH-RH) was studied. FSH-RH activity was not affected by trypsin, pepsin, neuraminidase, carboxy- peptidasc A, aminopeptidase M and leucine aminopcptidase. However, incubation with chymotrypsin, subtilisin, papain and pyrrolidonc carboxylyl peptidase abolished the FSH-RI1 activity as did treatment with hydrochloric acid (0.9 m, 1 h, 100°C), diazotized sulfanilic acid, and N-bromosuccinimide. Nitrous acid, sodium mctaperiodate, and ninhydrin did not affect the FSH-RII activity appreciably. Amino acid analyses of the purest FSH-RH preparation showed the following composition: His 1, Arg 1, Scr 1, Glu 1, Pro 1, Gly 2, Leu 1, Trp 1, and Tyr 1. These results and information obtained during purification procedures indicate that a basic polypeptide composed of ten amino acids possesses both LIl-RH and FSII-RH activity.

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KW - LH-releasing hormone

KW - Polypeptide

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