[Primary structure of the basic nuclear protein from spermatozoa of the mollusk Illex argentinus and its comparison with the structure of sperm proteins in other animals].

The spermatic protein of chromatin I2 of squid Illex argentinus was separated by HPLC into two components I2-1 and I2-2. Amino acid sequences of the major portion of protein I2-1 (52 residues) and the N-terminal sequence of protein I2-2 (21 residues) were determined. Arginines in protein I2-1 are arranged in clusters typical of protamines; the first cluster is in the N-terminus, the longest heterogeneous basic cluster is in the central part of the protein chain, the C-terminal part of the molecule contains two clusters of three hydroxyamino acids each.

[Primary structure of the OSCP-protein, conferring the oligomycin sensitivity to the H+-ATPase complex. II. Hydrolysis of OSCP with proteinase from Staphylococcus aureus and reconstruction of the polypeptide chain].

Hydrolysis of OSCP of bovine heart mitochondria by proteinase from Staphylococcus aureus V8 was followed by isolation of all individual peptides by means of gel-filtration and HPLC. Structural analysis of the peptides allowed to arrange BrCN-fragments and to reconstruct the complete amino acid sequence of the protein. Comparative structural analysis revealed existence of a certain homology between OSCP and delta- and b-subunits of the E.

Detailed structural analysis of exposed domains of membrane-bound Na+,K+-ATPase. A model of transmembrane arrangement.

Exposed regions of the alpha- and beta-subunits of membrane-bound Na+,K+-ATPase were in turn hydrolyzed with trypsin. Resistance of the beta-subunit to proteolysis was shown to be due mainly to the presence of disulfide bridge(s) in the molecule. A model for the spatial organisation of the enzyme in the membrane was proposed on the basis of detailed structural analysis of extramembrane regions of both subunits.

[A method of selective isolation of tryptophan- and cysteine-containing peptides by covalent chromatography. Analysis of the topography of the Na+,K+-ATPase alpha-subunit].

A procedure for highly selective isolation of tryptophan- and cysteine-containing peptides from protein hydrolysates has been developed on the basis of covalent chromatography. It includes incorporation of a thiol group into the tryptophan residues by sequential treatment of peptides with 2-nitrophenylsulfenyl chloride and beta-mercaptoethanol followed by immobilization on the corresponding supports via thiol-disulfide exchange. The technique is applicable to the analysis of the hydrolysate of the Na+, K+-ATPase alpha-subunit obtained by limited trypsinolysis of the membrane-bound enzyme.

Pig kidney Na+,K+-ATPase. Primary structure and spatial organization.

cDNAs complementary to pig kidney mRNAs coding for alpha- and beta-subunits of Na+,K+-ATPase were cloned and sequenced. Selective tryptic hydrolysis of the alpha-subunit within the membrane-bound enzyme and tryptic hydrolysis of the immobilized isolated beta-subunit were also performed. The mature alpha- and beta-subunits contain 1016 and 302 amino acid residues, respectively.

[Primary structure of the alpha subunit of Na+,K+-ATPase. I. Analysis of hydrophilic fragments of the polypeptide chain].

The selective tryptic digestion of the native membrane-bound enzyme was carried out under conditions that provide the extensive hydrolysis of hydrophilic regions of the alpha-subunit into small fragments and allow to preserve the integrity of the beta-subunit. Twenty-seven water-soluble peptides comprising approximately 40% of the total polypeptide chain were isolated by HPLC and their complete or partial amino acid sequence was determined. It led to general outline of the structural organisation of the alpha-subunit hydrophilic regions exposed from membrane.

[Primary structure of the OSCP protein that confers sensitivity to oligomycin on the mitochondrial H+-ATPase complex. I. Tryptic and cyanogen bromide peptides].

Trypsin and cyanogen bromide were used for cleavage of the OSCP preparations. The peptide mixtures thus formed were separated into individual components by a combination of various chromatographic procedures: gel filtration, ion exchange and paper chromatography, as well as reversed-phase HPLC. As a result, 31 tryptic peptides and 9 out of 10 possible cyanogen bromide peptides were isolated.

Oligomycin sensitivity-conferring protein (OSCP) of beef heart mitochondria. Internal sequence homology and structural relationship with other proteins.

Structural analysis of oligomycin sensitivity-conferring protein (OSCP) revealed repeating sequences (residues 1-89, 105-190) suggesting an evolution of the protein by gene duplication. In addition to the reported homology with the delta-subunit of Escherichia coli F1ATPase, OSCP also shows a certain homology with the b-subunit of E. coli F0 and the ADP/ATP carrier of mitochondria.

Amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria and its homology with the delta-subunit of the F1-ATPase of Escherichia coli.

The complete amino acid sequence of the oligomycin sensitivity-conferring protein (OSCP) of beef-heart mitochondria is reported. The protein contains 190 amino acids and has a molecular mass of 20 967. Its structure is characterized by a concentration of charged amino acids in the two terminal segments (N 1-77 and C 128-190) of the protein, whereas its central region is more hydrophobic.

[Primary structure of the dicyclohexylcarbodiimide-binding subunit of Streptococcus faecalis H+-ATPase].

The complete amino acid sequence of dicyclohexylcarbodiimide (DCC)-binding subunit of proton adenosine triphosphatase from glycolysing bacteria Streptococcus faecalis was established. Isolation of the protein from subbacterial particles was carried out by using extraction with a chloroform/methanol mixture and following gel-filtration on Sephadex LH-60 and Bio-gel P-30. To establish the primary structure, use was made of cyanogen bromide and hydroxylamine cleavages, trypsin and partial acid hydrolyses.

[Primary structure of cytoplasmic aspartate aminotransferase from pit heart muscle. Amino acid sequence of thermolytic peptides].

Amino acid sequences of 128 thermolytic peptides from carboxymethylated aspartate aminotransferase were determined. These peptides contain a total of 515 amino acid residues and account for a sequence of 384 amino acid residues in the aspartate aminotransferase.

[Primary structure of cytoplasmic aspartate aminotransferase from pig heart muscle. Amino acid sequence of peptides from cyanogen bromide hydrolysate].

Amino acid sequences were determined for the six peptides from cyanogen bromide hydrolysis of cytoplasmic aspartate aminotransferase. These peptides accounted for 177 amino acid residues of the enzyme. Partial sequence of N-terminal peptide accounting for 212 amino acid residues of enzyme was also determined.