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The luteinizing hormone of sperm whale isolation separation into subunits and study of amino acid sequence of the alpha subunit


, : The luteinizing hormone of sperm whale isolation separation into subunits and study of amino acid sequence of the alpha subunit. Biokhimiya 49(1): 111-126

The luteinizing hormone isolated from sperm whale pituitary was separated into 2 subunits, .alpha.- and .beta.-, by ion-exchange chromatography on sulfoethyl-Sephadex. The hormone subunits were reconstituted, carboxymethylated and cleaved by CNBr and proteolytic enzymes. To block tryptic hydrolysis at lysine residues the .alpha.-subunit was subjected to maleylation. Large-sized fragments of CNBr were cleaved by chymotrypsin and trypsin, while large-sized fragments of trypsin were split by chymotrypsin. The resulting peptides were separated by gel filtration on Sephadex, ion-exchange chromatography on Aminex A-5 and thin-layer partition chromatography on cellulose. The amino acid sequence of the peptides was determined by the Edman method, using identification of the N-terminal amino acids in a reaction with dansyl chloride or dimethylaminoazobenzene-4-isothiocyanate. The .alpha.-subunit of the luteinizing hormone is a peptide chain consisting of 96 amino acid residues with covalently linked carbon chains at asparagine residues at positions 56 and 82. The N-terminal amino acid of the .alpha.-subunit is phenylalanine, the C-terminal amino acid is serine. The .alpha.-subunit is heterogenous at the N-end, i.e., besides phenylalanine it contains threonine and trace amounts of proline, aspartate, glutamate and glycine.

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