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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. (Endocrinology75: 333, 1964)
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Adams-Mayne et al. (1964) studied this question.
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