Biomaterial Database

A Cl(-)-translocating adenosinetriphosphatase in Acetabularia acetabulum. 1. Purification and characterization of a novel type of adenosinetriphosphatase that differs from chloroplast F1 adenosinetriphosphatase. 1990

M Ikeda, and R Schmid, and D Oesterhelt

Faculty of Pharmaceutical Sciences, Okayama University, Japan.

ATPases were solubilized from membranes of Acetabularia acetabulum using nonanoyl-N-methylgluconamide and purified by ion-exchange and gel permeation chromatography. Three fractions of ATPase, Mono Q-I, -II, and -III, were separated. Activity in fraction Mono Q-I was very labile and could not be accurately determined. Fractions Mono Q-II and -III had specific activities of 0.6 and 6 units/mg of protein, respectively. By SDS-polyacrylamide gel electrophoresis, isoelectric focusing, and peptide mapping, it was shown that fractions Mono Q-II and -III consisted of the same polypeptides with molecular masses of 54K (a-subunit) and 50K (b-subunit). Fractions Mono Q-II and -III had the following catalytic properties: pH optimum at 6.0; substrate specificity, ATP = GTP = ITP much greater than UTP = CTP (Km for ATP 0.6 mM); divalent cation requirement, Mn2+ = Mg2+ greater than Co2+ greater than Zn2+ much greater than Ca2+, Ni2+. Both activities were inhibited by monovalent anions, while monovalent cations had neither inhibitory nor stimulatory effects. Orthovanadate inhibited both activities to 50% at 1 mM, and the most effective inhibitor of both was azide (95% inhibition at 100 microM). An enzyme-phosphate complex was formed after incubation of fraction Mono Q-III with [gamma-32P]ATP. The CF1-ATPase subcomplexes were isolated from the same organism and compared with the fraction Mono Q-III. Data supported the difference of fraction Mono Q-III from CF1-ATPase.

UI	MeSH Term	Description	Entries
D010449	Peptide Mapping	Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.	Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D011489	Protein Denaturation	Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.	Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002412	Cations	Positively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis.	Cation
D002712	Chlorides	Inorganic compounds derived from hydrochloric acid that contain the Cl- ion.	Chloride,Chloride Ion Level,Ion Level, Chloride,Level, Chloride Ion
D002736	Chloroplasts	Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.	Chloroplast,Etioplasts,Etioplast
D000076	Acetabularia	A genus of green algae found in the Mediterranean and other warm seas.	Acetabularias
D000251	Adenosine Triphosphatases	A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.	ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000460	Chlorophyta	A phylum of photosynthetic EUKARYOTA bearing double membrane-bound plastids containing chlorophyll a and b. They comprise the classical green algae, and represent over 7000 species that live in a variety of primarily aquatic habitats. Only about ten percent are marine species, most live in freshwater.	Algae, Green,Chlorophytina,Green Algae
D000838	Anions	Negatively charged atoms, radicals or groups of atoms which travel to the anode or positive pole during electrolysis.	Anion