[Amino acid sequence of myoglobin from seals from Lake Baikal].

The primary structure of myoglobin of the seal of Lake Baikal (East Siberia) Phoca siberica, determined by sequencing the whole protein and peptides obtained by the cyanogen bromide or proteinase cleavage and separated by the microcolumn liquid chromatography, was found to be identical to the primary structures of myoglobins of the harbour seal Phoca vitulina largha and the grey seal Halehoerus gryphus. It suggests that these species separated from a common ancestor less than seven million years ago.

[Use of electroblotting as a method for preparing samples of proteins and their fragments for microsequencing].

Gel electrophoresis in the presence of sodium dodecyl sulphate followed by electroblotting was employed in sample preparation for microsequencing proteins and protein fragments. Three types of solid supports were compared: glass fiber filters modified by aminopropyltriethoxysilane or covered with polybrene, and polyvinylidenedifluoride membranes. N-Terminal amino acid sequences of several proteins (Mr 14-140 kDA were determined on a gas-phase sequencer with the standard programme; 20-200 pmoles of the protein can be assayed by this method.

[Isolation and characteristics of cyanogen bromide peptides of transducin alpha and beta subunits].

The alpha- and beta-subunits of the GTP-binding protein (transducin) from cattle retina were cleaved with cyanogen bromide. 21 peptides covering 90-100% of the amino acid sequence of the alpha- and beta-subunits were isolated from the hydrolyzate. Cyanogen bromide peptides complete or partial amino acid sequence was determined, the results were compared with those by Numa and coworkers [1] and Lochrie et al.

[Primary structure of rhodopsin. II. Chymotrypsin hydrolysis peptides].

Apomembranes prepared from the photoreceptor disks were subjected to chymotryptic hydrolysis. The insoluble material, containing the membrane-bound peptides was removed by centrifugation, and the water-soluble peptides of the supernatant were separated by ion-exchange chromatography on AG 50W X 4 followed by high performance liquid chromatography. The insoluble peptides were separated by gel-filtration on Bio-Gel P-30 in 80% formic acid.