COMPARATIVE PEPTIDE MAPPING AND ISOELECTRIC FOCUSING OF ISOLATED SUBUNITS FROM CHICK EMBRYO BRAIN TUBULIN
Lynn P. Nelles
Department of Biochemistry, Colorado State University, Fort Collins, CO 80523, U.S.A.
The material presented in this paper is included in a dissertation for the Ph.D. degree from Colorado Stale University.
Marshfield Medical Foundation, Inc., 510 North St. Joseph Avenue, Marshfield, WI 54449. U.S.A.
Search for more papers by this authorCorresponding Author
James R. Bamburg
Department of Biochemistry, Colorado State University, Fort Collins, CO 80523, U.S.A.
Author to whom correspondence should be addressed. Address for 1 July 1978–30 June 1979: MRC Laboratory of Molecular Biology, University Postgraduate Medical School, Hills Road, Cambridge CB2 2QH, England.Search for more papers by this authorLynn P. Nelles
Department of Biochemistry, Colorado State University, Fort Collins, CO 80523, U.S.A.
The material presented in this paper is included in a dissertation for the Ph.D. degree from Colorado Stale University.
Marshfield Medical Foundation, Inc., 510 North St. Joseph Avenue, Marshfield, WI 54449. U.S.A.
Search for more papers by this authorCorresponding Author
James R. Bamburg
Department of Biochemistry, Colorado State University, Fort Collins, CO 80523, U.S.A.
Author to whom correspondence should be addressed. Address for 1 July 1978–30 June 1979: MRC Laboratory of Molecular Biology, University Postgraduate Medical School, Hills Road, Cambridge CB2 2QH, England.Search for more papers by this authorThe material presented in this paper is included in a dissertation for the Ph.D. degree from Colorado Stale University.
Marshfield Medical Foundation, Inc., 510 North St. Joseph Avenue, Marshfield, WI 54449. U.S.A.
Abstract—
The α- and β-subunits of chick embryo brain tubulin have been isolated under denaturing conditions and compared with respect to their molecular weight, amino acid composition, tryptic peptide maps, amide content and isoelectric focusing properties. An 8 M-Urea-containing polyacrylamide gel system with varying acrylamide concentrations was used for calculation of the retardation coefficients (KR) of the tubulin subunits. A molecular weight of 53,000 was estimated for each subunit by comparison to KR values for standard proteins. Amide contents of approx 41% of the carboxyl groups of α-tubulin and 48% of the carboxyl groups of β-tubulin were calculated using the average PI value, the pKintrinsic for the ionizable side chains of the amino acids and the amino acid composition of each subunit. Comparative peptide maps of trypsin digested α- and β-tubulin demonstrated 16 peptides unique to each subunit and 23 peptides which comigrate. Both subunits give rise to multiple species on electrofocusing gels. The average isoelectric points for the α- and β-subunits are 5.4 and 5.2, respectively.
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