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Evolutionary origin of numerous kringles in human and simian apolipoprotein(a)
Author(s) -
Ikeo Kazuho,
Takahashi Kei,
Gojobori Takashi
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80036-3
Subject(s) - kringle domain , serine protease , apolipoprotein b , biology , phylogenetic tree , amino acid , serine , protease , microbiology and biotechnology , genetics , biochemistry , enzyme , gene , recombinant dna , cholesterol
Human apolipoprotein(a) has a great size heterogeneity and consists of 38 kringle domains in the amino terminal and a serine proteasc domain in the carboxyl terminal. All but one kringle of apolipoprotein(a) are homologous to the fourth kringle of plasminogen. However, the 38th kringle resembles the fifth kringle of plasminogen and it seems to have been deleted in simian species. The phylogenetic trees suggest that an ancestral apolipoprotein(a) may have started with a duplicate of a plasminogen type protein. It also implies that deletion of the three kringles in the amino terminus followed, and that one of the remaining two kringles was duplicated in both human and simian species and the other was processed by a deletion in simian species after species separation. Thus, the number of kringles in other mammals not yet studied may vary considerably from species to species.