Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Statistics
  • Help & Advice
University of Warwick

The Library

  • Login

PURIFICATION OF RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE AND OF CARBOXYSOMES FROM THIOBACILLUS-THYASIRIS THE PUTATIVE SYMBIONT OF THYASIRA-FLEXUOSA (MONTAGU)

Tools
- Tools
+ Tools

UNSPECIFIED (1991) PURIFICATION OF RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE AND OF CARBOXYSOMES FROM THIOBACILLUS-THYASIRIS THE PUTATIVE SYMBIONT OF THYASIRA-FLEXUOSA (MONTAGU). ARCHIVES OF MICROBIOLOGY, 156 (5). pp. 338-343. ISSN 0302-8933

Full text not available from this repository.

Abstract

The bacterial symbionts of many marine invertebrates contain ribulose 1,5-bisphosphate (RuBP) carboxylase but apparently no carboxysomes, polyhedral bodies containing RuBP carboxylase. In the few cases where polyhedral bodies have been observed they have not been characterised enzymatically. Polyhedral bodies, 50-90 nm in diameter, were observed in thin cell sections of Thiobacillus thyasiris the putative symbiont of Thyasira flexuosa and RuBP carboxylase activity was detected in both soluble and particulate fractions after centrifugation of cell-free extracts. RuBP carboxylase purified 90-fold from the soluble fraction was of high molecular weight and consisted of large and small subunits, with molecular weights of 53,110 and 11,100 respectively. Particulate RuBP carboxylase activity was associated with polyhedral bodies 50-100 nm in diameter, as revealed by density gradient centrifugation and electron microscopy. Therefore, the polyhedral bodies were inferred to be carboxysomes. Native electrophoresis of isolated carboxysomes demonstrated a major band which comigrated with the purified RuBP carboxylase and three minor bands of lower molecular weight. Sodium dodecylsulphate (SDS) gel electrophoresis of SDS-dissociated carboxysomes demonstrated nine major polypeptides two of which were the large and small subunits of RuBP carboxylase. The RuBP carboxylase subunits represented 21% of the total carboxysomal protein. The most abundant polypeptide had a molecular weight of 40,500. Knowledge of carboxysome composition is necessary to provide an understanding of carboxysome function.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Journal or Publication Title: ARCHIVES OF MICROBIOLOGY
Publisher: SPRINGER VERLAG
ISSN: 0302-8933
Date: October 1991
Volume: 156
Number: 5
Number of Pages: 6
Page Range: pp. 338-343
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/22420

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item View Item
twitter

Email us: publications@warwick.ac.uk
Contact Details
About Us