TRANSCARBOXYLASE, VIII. ISOLATION AND PROPERTIES OF A BIOTIN-CARBOXYL CARRIER PROTEIN*

  1. Brenda I. Gerwin†,
  2. Birgit E. Jacobson, and
  3. Harland G. Wood
  1. DEPARTMENT OF BIOCHEMISTRY, CASE WESTERN RESERVE UNIVERSITY, CLEVELAND, OHIO

Abstract

Methylmalonyl CoA-oxalacetate transcarboxylase (EC 2. 1. 3. 1) from Propionibacterium shermanii is a biotin enzyme of 670,000 molecular weight containing 6 moles of biotin per mole of enzyme. The active enzyme dissociates spontaneously at low ionic strength and alkaline pH to a mixture of inactive subunits. One type of subunit contains all the biotin of the original molecule. The biotin unit has an S20,w = 1.3S and a molecular weight of approximately 12,000. It contains 1 mole of biotin and 1 half-cystine per mole. Qualitative dansyl techniques indicate that alanine is the amino terminal residue of the biotin subunit.

Footnotes

  • ↵ † Present address: Mann Program, Rockville Laboratory, 540 Fisher Lane, Rockville, Maryland 20852.

  • ↵ * This investigation was supported by grants GM11839 and AM12245 from the National Institutes of Health.

« Previous | Next Article »Table of Contents

This Article

  1. PNAS 1969-12 vol. 64 no. 4 1315-1322
  1. » Abstract
  2. Full Text (PDF)
About Our New Site Design >>
Link: Advanced Search

This Week's Issue

  1. August 19, 2008, 105 (33)
  1. Current Issue
  1. Alert me to new issues of PNAS

Most