Answers are grounded in this paper and cite their sources.
The primary structure of porcine luteinizing hormone α‐subunit was established by determination of the amino acid sequence of its tryptic peptides, which were aligned by homology with the known sequence of ovine luteinizing hormone α‐subunit. Its polypeptide chain is shorter by six amino acid residues at its amino‐terminus, when compared to the ovine α‐subunit. Furthermore four amino acid replacements are observed in the porcine as compared with the ovine chain. Heterogeneity of both carbohydrate prosthetic groups of porcine luteinizing hormone α‐subunit is indicated by the different sugar compositions of the glycopeptides isolated in the course of this work.
No takes yet. Share an insight, caveat, or question.
Maghuin‐Rogister et al. (1973) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: