The domain structure of the inhibitor subunit of human inter-alpha-trypsin inhibitor reflects the exon structure of its gene.
The gene coding for the inhibitor subunit of the human plasma protein complex inter-alpha-trypsin inhibitor has been cloned. The exon structure of the gene corresponds with the organization of the protein in two distinct inhibitor domains. The exons coding for the inhibitor domains each comprise the complete information for a typical Kunitz-type proteinase inhibitor structure. In contrast to bovine aprotinin, the mature inhibitor protein contains amino acid residues flanking the inhibitor domains on both sides. These amino acid residues are encoded by additional exons.
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Abteilung für Klinische Chemie und Klinische Biochemie, Universität München, FRG.
Kögler
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Gebhard
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D000510:Alpha-Globulins / Q000235:genetics*; D000595:Amino Acid Sequence; D007611:Aprotinin / Q000235:genetics; D001483:Base Sequence; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D003001:Cloning, Molecular; D015246:Deoxyribonuclease EcoRI; D005091:Exons; D006801:Humans; D008969:Molecular Sequence Data; D009693:Nucleic Acid Hybridization; D015345:Oligonucleotide Probes; D014361:Trypsin Inhibitors
D000510:Alpha-Globulins; D015345:Oligonucleotide Probes; D014361:Trypsin Inhibitors; C011877:inter-alpha-inhibitor; D007611:Aprotinin; D015246:Deoxyribonuclease EcoRI; D002918:Chymotrypsin