Plasminogens Tochigi II and Nagoya: Two Additional Molecular Defects with Ala-600 → Thr Replacement Found in Plasmin Light Chain Variants 123 (original) (raw)
Journal Article
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Department of Biology, Faculty of Science, Kyushu University 33
Higashi-ku, Fukuoka, Fukuoka 812
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Department of Biology, Faculty of Science, Kyushu University 33
Higashi-ku, Fukuoka, Fukuoka 812
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Department of Medicine and Institute of Hematology, Jichi Medical School
Tochigi 329-04
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Department of Medicine and Institute of Hematology, Jichi Medical School
Tochigi 329-04
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Department of Internal Medicine, Nagoya University School of Medicine
Showa-ku, Nagoya, Aichi 446
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Department of Internal Medicine, Nagoya University School of Medicine
Showa-ku, Nagoya, Aichi 446
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Published:
01 August 1984
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Toshiyuki MIYATA, Sadaaki IWANAGA, Yoichi SAKATA, Nobuo AOKI, Junki TAKAMATSU, Tadashi KAMIYA, Plasminogens Tochigi II and Nagoya: Two Additional Molecular Defects with Ala-600 → Thr Replacement Found in Plasmin Light Chain Variants , The Journal of Biochemistry, Volume 96, Issue 2, 1984, Pages 277–287, https://doi.org/10.1093/oxfordjournals.jbchem.a134836
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Abstract
Previous studies in our laboratories (Miyata, T., et al . (1982) Proc. Natl. Acad. Sci. U.S.79 , 6132–6136) showed that the structural defect in a hereditarily abnormal plasminogen, plasminogen Tochigi, is due to replacement of Ala by Thr at position 600 from the NH 2 -terminal end. In the present studies, two abnormal plasminogens, plasminogens Tochigi II and Nagoya, obtained from other family members were analyzed to identify the structural impairment in these molecules. Amino acid sequence analysis of one of the tryptic peptides isolated, respectively, from plasminogens Tochigi I[ and Nagoya indicated that in both cases, Ala-600 (equivalent to Ala-55 of the chymotrypsin numbering system) had been replaced by Thr. No other substitutions at the active site and substrate-binding site residues, namely, His-57, Asp-102, Ser-195, and Asp-189, were found in the plasmin light chain variants, indicating that all these residues are intact. Moreover, the NH2-terminal heptapeptide sequences of the plasmin light chain variants isolated from plasminogens Tochigi II and Nagoya were identical to the sequence determined for the normal control. These results indicate that the absence of proteolytic activity of both abnormal molecules is due to the same amino acid substitution as that of previously reported plasminogen Tochigi.
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Topic:
- amino acid substitution
- antigens, cd98 light chains
- chymotrypsin
- laboratory
- peptides
- plasmin
- plasminogen
- sequence analysis, protein
- spinal cord injuries
- threonine
- proteolysis
- molecule
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