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• W2073204417 abstract "Ovine luteinizing hormone has been subjected to partial digestion by trypsin to obtain two major glycoprotein fractions with dissimilar carbohydrate moieties, plus a number of simple peptides. The glycoproteins were separated by gel filtration on Sephadex G-50, then digested with pronase to obtain small glycopeptides containing 3 to 6 amino acids. The latter peptides were further purified by gel filtration and DEAE-cellulose ion exchange chromatography. Composition and peptide sequence of the small glycopeptides are indicated. The analyses suggest a heterogeneity for the glycopeptides isolated. This heterogeneity is due in part to heterogeneity in the carbohydrate portion of the hormone initially- isolated plus differences in the point of cleavage of the peptide chain by pronase employed in the degradation." @default.
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• W2073204417 date "1968-10-01" @default.
• W2073204417 modified "2023-10-17" @default.
• W2073204417 title "Trypsin digestion of native ovine luteinizing hormone and studies on the glycopeptide fragments" @default.
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• W2073204417 doi "https://doi.org/10.1016/0016-6480(68)90099-3" @default.
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