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Stability Studies on Luteinizing Hormone

Name: Stability Studies on Luteinizing Hormone
Keywords: Clostridium, Hot Temperature, Chemical Phenomena, Formates, Neuraminidase, Ascorbic Acid, Carboxypeptidases, Hydrogen-Ion Concentration, Luteinizing Hormone, Guanidines

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 1964 English Publisher:The Endocrine SocietyJournal:Endocrinology, volume 75, pages 333-340 (issn: 0013-7227, eissn: 1945-7170,

Authors: Mabelle Adams-Mayne; Darrell N. Ward;

doi: 10.1210/endo-75-3-333

pmid: 14235400

Stability Studies on Luteinizing Hormone

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Abstract

Stability of the biological activity of luteinizing hormone to a range of conditions and agents was studied using the Parlow ovarian ascorbic acid depletion assay. Inactivation was virtually complete after performic acid oxidation, urea denaturation, heating to 100 C in solution, subjection to pH 2 at 25 C or less, reduction by sodium in liquid ammonia, or digestion by the enzymes trypsin or clostripaine. Partial inactivation was observed after limited digestion with chymotrypsin, trypsin, carboxypeptidase A, clostripaine, or incubation with sulfhydrylcontaining compounds. No inactivation was observed following neuraminidase or bacterial a-amylase treatment or short exposure to pH 12. (Endocrinology 75: 333, 1964)

Related Organizations

The University of Texas at Austin
United States

Keywords

Clostridium, Hot Temperature, Chemical Phenomena, Formates, Neuraminidase, Ascorbic Acid, Carboxypeptidases, Hydrogen-Ion Concentration, Luteinizing Hormone, Guanidines, Chemistry, Amylases, Animals, Chymotrypsin, Humans, Biological Assay, Cattle, Dimercaprol, Female, Cysteine

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