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. 1969 Dec;64(4):1315–1322. doi: 10.1073/pnas.64.4.1315

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

Brenda I Gerwin 1,†, Birgit E Jacobson 1, Harland G Wood 1
PMCID: PMC223285  PMID: 5271754

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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