Partial amino acid sequence of calmodulin-independent bovine brain adenylate cyclase.
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Adenylyl Cyclases↗
Biomedical subjects
Ovchinnikov YuA
Publications and source records attributed to Ovchinnikov YuA.
Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein.
The primary structure of a gene of the Na+, K+-ATPase multigenic family in the human genome has been determined. The gene corresponds to a hypothetical alpha III-form of the enzyme catalytic subunit. The gene comprises over 25,000 bp, and its protein coding region includes 23 exons and 22 introns. Possible correlation between structural features of the protein and location of introns in the gene are discussed.
Amino Acid Sequence↗
Photosynthetic reaction centre of Chloroflexus aurantiacus. Primary structure of M-subunit.
The M-subunit primary structure of the reaction centre (RC) from Chloroflexus aurantiacus composed of 306 amino acid residues has been determined by parallel analysis of the protein and corresponding DNA. The blocked N-terminus as well as replacement of the essential histidine liganding Mg of an accessory bacteriochlorophyll in purple bacteria by leucine distinguishes the M-subunit of Chloroflexus RC from that of purple bacteria.
Amino Acid Sequence↗
Octopus rhodopsin. Amino acid sequence deduced from cDNA.
The primary structure of rhodopsin from the octopus Paroctopus defleini has been determined by parallel analysis of the protein and corresponding cDNA. The amino acid sequence is most similar to the recently cloned Drosophila opsins. Similarities to bovine and human opsins are also evident. The transmembrane topology of octopus rhodopsin is discussed.
Amino Acid Sequence↗
Photosynthetic reaction centre of Chloroflexus aurantiacus. I. Primary structure of L-subunit.
The L-subunit primary structure of the reaction centre from Chloroflexus aurantiacus composed of 310 amino acid residues has been determined by parallel analysis of the protein and corresponding DNA. Significant homology between this protein and L-subunits from reaction centres of purple bacteria is observed. This implies close similarity in the tertiary structure of these proteins.
Amino Acid Sequence↗
Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated.
Covalent coupling of bovine rhodopsin to CPG-thiol glass was used for separation of CNBr peptides. It is shown that cysteine residues 322 and 323 in the C-terminal cytoplasmic fragment of rhodopsin are modified with palmitic acid.
Acylation↗
Topology of Na+,K+-ATPase. Identification of the extra- and intracellular hydrophilic loops of the catalytic subunit by specific antibodies.
To study the topology of Na+,K+-ATPase monoclonal antibodies (MAbs) specific for membrane-bound enzyme were produced. Using immunofluorescence staining of viable cells or smears of a pig kidney embryonic (PKE) cell line, two groups of MAbs were selected, namely those binding to extra- or intracellular portions of the alpha-subunit. The extracellular location of peptide loop 804-841 linking the Vth and VIth intramembrane hydrophobic segments was proved using MAb VG2. Another MAb, IIC9, interacting with PKE cells only after membrane perforation (4% formaldehyde and 0.1% Tween-20), was shown to bind to the hydrophilic loop 868-945. The antigenic determinants recognized by MAb IIC9 and VG2 are located in peptides 887-904 and 810-825, respectively. The C-terminus of the alpha-subunit molecule was positioned on the outer side of the cytoplasmic membrane utilizing affinity-purified antibodies to the synthetic peptide corresponding to fragment 999-1008.
Amino Acid Sequence↗
Differentiated analysis of the secondary structure of hydrophilic and hydrophobic regions in alpha- and beta-subunits of Na+,K+-ATPase by Raman spectroscopy.
Raman spectra of active Na+,K+-ATPase from pig kidney and membrane-bound products of its two-stage trypsinolysis, including alpha-subunit hydrophobic regions as well as the intact beta-subunit and hydrophobic regions of alpha- and beta-subunits, were measured to calculate the secondary structure of hydrophilic and hydrophobic regions of the enzyme. Consequent comparison demonstrated unambiguously that (i) membrane-bound hydrophobic parts of polypeptide chains of Na+,K+-ATPase subunits are in the alpha-helical conformation; (ii) essential contents of the alpha-helix as well as beta-sheet are estimated to form the hydrophilic (mainly cytoplasmic) domain of the Na+,K+-ATPase alpha-subunit; (iii) the exoplasmic hydrophilic domain of the beta-subunit is shown to include several antiparallel beta-pleated sheets and a small amount of the alpha-helix and unordered conformations. The model of the secondary structure organization of hydrophilic domains as well as 8 hydrophobic transmembrane segments of the enzyme molecule was proposed on the basis of experimental results and predictional calculations.
Animals↗
Primary structure of bovine cerebellum GTP-binding protein G39 and its effect on the adenylate cyclase system.
The primary structure of bovine cerebellum GTP-binding protein alpha-subunit, protein G39, was determined by parallel analysis of the protein amino acid sequence and the corresponding cDNA nucleotide sequence. The protein consists of 354 amino acid residues and has a molecular mass of 40064 Da. High homology between G39 and other G-proteins, especially rat brain G0, was shown. An assumption is made that certain brain adenylate cyclase system properties are determined by the presence of G39.
Adenylyl Cyclases↗
Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of the alpha-subunit and nucleotide sequence of the corresponding cDNA.
The alpha-subunit primary structure of cyclic GMP phosphodiesterase has been determined by parallel analysis of the protein amino acid sequence and the corresponding cDNA nucleotide sequence. The enzyme alpha-subunit contains 858 amino acid residues, its N-terminal amino group being acetylated. The partial primary structure of the enzyme beta-subunit has also been elucidated. A significant homology has been found between the alpha- and beta-subunits of cGMP phosphodiesterase.
3',5'-Cyclic-GMP Phosphodiesterases↗
Family of Na+,K+-ATPase genes. Intra-individual tissue-specific restriction fragment length polymorphism.
Intra-individual tissue-specific restriction fragment length polymorphism (RFLP) has been demonstrated in DNA isolated from different mammalian tissues using cDNAs of alpha- and beta-subunits of Na+,K+-ATPase as hybridization probes. We propose that the RFLPs could result from gene rearrangements in the gene loci for the alpha- and beta-subunits of Na+,K+-ATPase. The changes in restriction patterns have been shown to occur during embryonic development and tumor formation. In addition, the tissue specificity of the expression of different genes of the family of Na+,K+-ATPase genes and their low expression in tumor cells have been demonstrated.
Animals↗
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.
Amino Acid Sequence↗
Chromosomal localization of the gene coding for alpha-subunit of Na+,K+-ATPase in the American mink (Mustela vison).
The gene coding for the alpha-subunit of Na+,K+-ATPase has been localized on chromosome 2 of the American mink (Mustela vison) using the somatic cell hybrids mink-Chinese hamster and pig cDNA clones as hybridization probes.
Animals↗
Affinity modification of E1-form of Na+, K+-ATPase revealed Asp-710 in the catalytic site.
An alkylating ATP analogue, gamma-[4-(N-2-chlorethyl-N-methylamino)]benzylamide ATP (C1RATP), covalently binds to the catalytic alpha-subunit of Na+, K+-ATPase yielding a product resistant to hydrolysis by the enzyme and inhibiting the ATP-hydrolysing activity. The Na+-form of the membrane-bound Na+, K+-ATPase modified with C1RATP was hydrolysed by pepsin under conditions providing maximum stability of the modification product (4 degrees C, pH 1.5). The modified peptide was isolated by HPLC and its amino acid sequence was found to involve residues 706-713 of the alpha-subunit polypeptide chain. This fragment located near the gamma-phosphate of ATP is a component of the active site. It is highly homologous with corresponding regions of the catalytic subunits of all the known E1-E2 ATPases. In the Na+-(or E1-)enzyme form Asp-710 is the target of modification. Evidently E1- and E2-enzymes have different targets in C1RATP modification, i.e. the polypeptide chain regions near the ATP gamma-phosphate in the enzyme active site differ somewhat in their conformations.
Adenosine Triphosphatases↗
The family of human Na+,K+-ATPase genes. A partial nucleotide sequence related to the alpha-subunit.
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Amino Acid Sequence↗
Application of new catalytic phosphate protecting groups for the highly efficient phosphotriester oligonucleotide synthesis.
An effective procedure for the synthesis of oligonucleotides by the phosphotriester method has been developed. The procedure is based on the use of phosphate protecting groups enabling O-nucleophilic intramolecular catalysis in the reaction of internucleotide bond formation under the action of arylsulfonyl chlorides and their derivatives. Using this new procedure, the time needed to perform one elongation step on polymer support is 7-8 min. The effectiveness of the methodology has been demonstrated in the synthesis of many oligodeoxyribonucleotides of different length with high yields.
Base Sequence↗
Cyclic GMP phosphodiesterase from cattle retina. Amino acid sequence of the gamma-subunit and nucleotide sequence of the corresponding cDNA.
The primary structure of the gamma-subunit of cyclic GMP phosphodiesterase was determined by parallel analysis of the amino acid sequence of the protein and nucleotide sequence of the corresponding cDNA. The enzyme gamma-subunit contains 87 amino acid residues, its N-terminal amino group being acetylated.
3',5'-Cyclic-GMP Phosphodiesterases↗
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. Structural data on the peptides from extramembrane regions of the alpha-subunit and on glycopeptides of the beta-subunit underlie a model for the transmembrane arrangement of Na+,K+-ATPase polypeptide chains.
Amino Acid Sequence↗