The chemistry of the adrenocorticotropins and the melanotropins

Oelofsen, Willem

doi:10.1016/0306-039x(75)90050-1

Cited by 2 publications

(3 citation statements)

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“…In any event, ostrich corticotropin seems to exhibit a more basic character than corticotropin from other species with pl values ranging from 7 to 8. The N-terminal amino acid of peak-8b' material from both fresh and aged glands was identified as serine, which is in accordance with that from other species (Oelofsen, 1975). The results of the amino acid analysis of 20h hydrolysates of each purified preparation are shown in Table 2.…”

Section: Results and Discussion Isolation Proceduressupporting

confidence: 79%

“…The different pl values observed could possibly be explained in terms of a variation in amide content between the hormone preparations from fresh and aged glands. Corticotropin preparations previously isolated from different species were found to contain at most two amide groups per molecule (Oelofsen, 1975). In the ostrich the most basic (pl 8.7) component, predominating in the preparation from fresh glands, could represent such a diamide variant.…”

Section: Results and Discussion Isolation Proceduresmentioning

confidence: 99%

“…Of the various polypeptide and protein hormones produced by the pituitary gland, corticotropin (ACTH) was one ofthe first to be isolated in pure form from a variety of species, including pigs, sheep, cattle and man, and more recently from the dogfish Squalus acanthias (Oelofsen, 1975). All these corticotropin preparations show much similarity in terms of both chemical structure and biological activity.…”

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The isolation and characterization of corticotropin from the pituitary gland of the ostrich Struthio camelus

Naudé¹,

Oelofsen²

1977

Biochemical Journal

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1. Avian corticotropin (ACTH) was purified from both fresh and aged pituitary glands of the ostrich Struthio camelus. 2. The isolation of corticotropin in pure form involved acid/acetone extraction, NaCl fractionation, CM-cellulose chromatography and Sephadex G-50 chromatography. 3. The hormone preparations from fresh and aged glands behaved as single substances on polyacrylamide-gel electrophoresis, and both preparations were found to consist of 39 amino acid residues, in identical molar proportions for the different amino acids. 4. The isoelectric points of the two hormone preparations were estimated to be in the range pH 8.3-8.7, indicating possible differences in amide content, and the N-terminal amino acid of both preparations appeared to be serine. 5. The hormone preparations from fresh and aged glands exhibited similar biological potencies (73 and 77 i.u./mg respectively), as measured by steroidogenesis in vitro. 6. Apart from possible differences in amide content, the corticotropin preparations obtained from fresh and aged glands appear to be indistinguishable.

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Section: Results and Discussion Isolation Proceduressupporting

confidence: 79%

Section: Results and Discussion Isolation Proceduresmentioning

confidence: 99%

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