Evidence of homology between the β-chain of human haptoglobin and the chymotrypsin family of serine proteases

Alexander Kurosky, Don R. Barnett, Marily A. Rasco, Tong Ho Lee, Barbara H. Bowman

    Research output: Contribution to journalArticle

    18 Citations (Scopus)

    Abstract

    Amino acid sequences from the β-chain of human haptoglobin are compared with those sequences known for the serine proteases of the chymotrypsin family. In a comparison of some 171 residues of the haptoglobin β-chain (approximately 60% of the protein molecule), approximately 30% of these are identical to residues occurring in sequences of either bovine trypsin, bovine chymotrypsin A, bovine chymotrypsin B, porcine elastase, or bovine thrombin B-chain, and an additional 10% are chemically similar. A combined comparison of the haptoglobin β-chain with the above five serine proteases gave an identity of 56% and a chemical similarity of 11%. Similarity of primary structure is also striking around two of the five half-cystinyl residues so far characterized in long lengths of sequence. These data provide substantial evidence that the β-chain of haptoglobin is homologous to the chymotrypsin family of serine proteases. Proposals are also presented to explain the occurrence of internal homology in the N-terminal region of the β-chain.

    Original languageEnglish (US)
    Pages (from-to)279-293
    Number of pages15
    JournalBiochemical Genetics
    Volume11
    Issue number4
    DOIs
    StatePublished - Apr 1974

    Fingerprint

    Haptoglobins
    haptoglobins
    Chymotrypsin
    Serine Proteases
    chymotrypsin
    serine proteinases
    homology
    cattle
    Pancreatic Elastase
    Thrombin
    Trypsin
    elastase
    thrombin
    trypsin
    Amino Acids
    Amino Acid Sequence
    Molecules
    Swine
    amino acid sequences
    amino acid

    Keywords

    • amino acid sequences
    • chymotrypsin
    • elastase
    • haptoglobin
    • plasmin
    • protein homology
    • serine proteases
    • thrombin
    • trypsin

    ASJC Scopus subject areas

    • Genetics
    • Biochemistry

    Cite this

    Evidence of homology between the β-chain of human haptoglobin and the chymotrypsin family of serine proteases. / Kurosky, Alexander; Barnett, Don R.; Rasco, Marily A.; Lee, Tong Ho; Bowman, Barbara H.

    In: Biochemical Genetics, Vol. 11, No. 4, 04.1974, p. 279-293.

    Research output: Contribution to journalArticle

    Kurosky, Alexander ; Barnett, Don R. ; Rasco, Marily A. ; Lee, Tong Ho ; Bowman, Barbara H. / Evidence of homology between the β-chain of human haptoglobin and the chymotrypsin family of serine proteases. In: Biochemical Genetics. 1974 ; Vol. 11, No. 4. pp. 279-293.
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    N2 - Amino acid sequences from the β-chain of human haptoglobin are compared with those sequences known for the serine proteases of the chymotrypsin family. In a comparison of some 171 residues of the haptoglobin β-chain (approximately 60% of the protein molecule), approximately 30% of these are identical to residues occurring in sequences of either bovine trypsin, bovine chymotrypsin A, bovine chymotrypsin B, porcine elastase, or bovine thrombin B-chain, and an additional 10% are chemically similar. A combined comparison of the haptoglobin β-chain with the above five serine proteases gave an identity of 56% and a chemical similarity of 11%. Similarity of primary structure is also striking around two of the five half-cystinyl residues so far characterized in long lengths of sequence. These data provide substantial evidence that the β-chain of haptoglobin is homologous to the chymotrypsin family of serine proteases. Proposals are also presented to explain the occurrence of internal homology in the N-terminal region of the β-chain.

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