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):

Report Date:

1970-07-30

Pagination or Media Count:

158.0

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

Subject Categories:

  • Biochemistry
  • Microbiology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE