JBC, Vol. 252, Issue 2, 639-643, Jan, 1977
The covalent structure of cartilage collagen. Evidence for sequence heterogeneity of bovine alpha1(II) chains
W. T. Butler, J. E. Finch Jr and E. J. Miller
During studies on the amino acid sequence of bovine nasal cartilage
collagen, the cyanogen bromide peptide alpha1(II)-CB11 was degraded to
smaller peptides with trypsin. One of the tryptic peptides, T5, which
contained 39 residues was shown by amino acid and sequence analyses to
occur in a predominant form that contained glutamine at position 5 and in a
second form with leucine at this site. In addition to the heterogeneity at
this position, amino acid analyses of five different preparations revealed
that the peptide with leucine contained a seryl residue not found in the
major form. Sequence heterogeneity at a third position of alpha1(II) was
demonstrated by the isolation of a hexapeptide (T2) from the trypsin digest
of alpha1(II)-CB11 which contained 0.21 residue of alanine and 0.77 of
leucine. Both the leucine and alanine of T2 were removed after the second
cycle of subtractive Edman degradation. These data show that at least two
types of alpha1(II) chains, designated as alpha1(II)Major and
alpha1(II)Minor, exist in bovine nasal cartilage. Further considerations
suggest that these two chains are probably not variants derived from
allelic genes but are the products of separate genes.
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