Accession Number : AD0712844
Title : HALOPHILIC BACTERIA.
Descriptive Note : Final rept. 1 Jul 67-30 Jun 70,
Corporate Author : BERGEN UNIV (NORWAY) DEPT OF BIOCHEMISTRY
Personal Author(s) : Dundas,Ian E. D.
Report Date : 30 JUL 1970
Pagination or Media Count : 158
Abstract : Ornithine Carbamoyl Transferase from Halobacterium salinarium has been purified. This enzyme is irreversibly inactivated in the absence of salt and the whole purification procedure, preparation of cell-free extracts, acetone fractionation, gel filtration, sucrose gradient centrifugation and chromatography on calcium phosphate gel was carried out in the presence of 4.3 M NaCl. The enzymatic properties of the purified Ornithine Carbamoyl Transferase were studied and compared to those of Ornithine Carbamoyl Transferase from non-halophilic organisms. The halophilic enzyme is composed of subunits with a molecular weight of about 75,000. Prolonged dialysis against NaCl free media resulted in a drastic decrease of the sedimentation velocity for the protein. The enzyme contains high relative concentrations of acidic amino acids; Flagella from Halobacteria have a marked tendency to aggregate in spiral structures visible with the light microscope. A method for staining the flagella has been developed. All Halobacteria isolated to date have complex nutritional requirements. A method for isolating Halobacteria with simple growth requirements is described. (Author)
Descriptors : (*PSEUDOMONADACEAE, *ENZYMES), PURIFICATION, BACTERIA, AMINO ACIDS, PROTEINS, NUTRITION, PHYSIOLOGY, CHEMICAL PROPERTIES, SALTS, SALINITY, ENVIRONMENT, NORWAY
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE