The amino acid sequence of the N-terminal two-thirds of a trout high-mobility-group protein, HMG-T, has been determined as a continuous sequence of 174 residues out of a total for the whole molecule of 260 residues. When this sequence was compared with published sequences of long cyanogen bromide-derived peptides from the analogous calf-thymus proteins, HMG-1 and −2 (Walker et al., 1979), there was strong homology, with 60–70% identity of corresponding amino acid residues in the three proteins, the majority in lengthy identical runs. However, a discrepancy in the position of a highly acidic run of aspartic and glutamic residues suggests this region may not lie within the main polypeptide chain but may represent a separate chain or possibly a branched structure,
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February 01 1981
Amino acid sequence homologies between the high-mobilitygroup proteins, HMG-T from trout testis and HMG-1 and-2 from calf thymus: is the poly-aspartic-glutamic acid polypeptide within the main chain?
D. C. Watson;
D. C. Watson
1Department of Medical Biochemistry, Faculty of Medicine, The University of Calgary, Calgary, Alberta, Canada T2N 1N4
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G. H. Dixon
G. H. Dixon
1Department of Medical Biochemistry, Faculty of Medicine, The University of Calgary, Calgary, Alberta, Canada T2N 1N4
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Publisher: Portland Press Ltd
Received:
February 02 1981
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1981 The Biochemical Society
1981
Biosci Rep (1981) 1 (2): 167–175.
Article history
Received:
February 02 1981
Citation
D. C. Watson, G. H. Dixon; Amino acid sequence homologies between the high-mobilitygroup proteins, HMG-T from trout testis and HMG-1 and-2 from calf thymus: is the poly-aspartic-glutamic acid polypeptide within the main chain?. Biosci Rep 1 February 1981; 1 (2): 167–175. doi: https://doi.org/10.1007/BF01117014
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