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- W242118340 abstract "Rabbit histidine-rich glycoprotein (HRG) circulates as a 94000 molecular weight protein but can be rapidly cleaved by plasmin to at least three glycopeptides which are cross-linked by disulfide bonds. Even after reduction and carboxymethylation, a portion of the cleaved molecules chramatograph like the intact molecule, indicating that strong non-covalent intra-molecular forces exist. One fragment (molecular weight ca. 30000) has been isolated by reverse-phase HPLC and found to contain a high proportion of proline (23.6%), glycine (18.3%), and histidine (20.1%). A similar peptide has been derived from human HRG. This portion of the HRG molecule may well account for the unusual metal binding properties of HRG as well as help explain its biological function." @default.
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- W242118340 date "1984-01-01" @default.
- W242118340 modified "2023-10-16" @default.
- W242118340 title "Interaction of the Histidine-Rich Glycoprotein of Serum with Metals and Plasmin" @default.
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- W242118340 doi "https://doi.org/10.1016/b978-0-08-030764-0.50009-4" @default.
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