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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 of sperm whale isolation separation into subunits and study of amino acid sequence of the alpha subunit
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.


Accession: 006712463



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