Open AccessBiotin Carboxyl Carrier Protein in Barley Chloroplast Membranes
Author(s) -
KANNANGARA C. Gamini,
JENSEN C. John
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb04109.x
Subject(s) - biotin , chloroplast , biochemistry , mole , covalent bond , acetyl coa carboxylase , chemistry , membrane , acetic acid , pyruvate carboxylase , urea , avidin , enzyme , organic chemistry , gene
Biotin localized in barley chloroplast lamellae is covalently bound to a single protein with an approximate molecular weight of 21000. It contains one mole of biotin per mole of protein and functions as a carboxyl carrier in the acetyl‐CoA carboxylase reaction. The protein was obtained by solubilization of the lamellae in phenol/acetic acid/8 M urea. Feeding barley seedlings with [ 14 C]‐biotin revealed that the vitamin is not degraded into respiratory substrates by the plant, but is specifically incorporated into biotin carboxyl carrier protein.