| Literature DB >> 1382603 |
M S Liu1, Y Ma, M R Hayden, J D Brunzell.
Abstract
A monoclonal antibody, 5D2, which inhibits human lipoprotein lipase (hLPL) activity has been widely used for assessment of LPL immunoreactive mass in the clinical evaluation of patients [1] and for analysis of structure-function relationships of LPL [2,3]. We have mapped the epitope on LPL, recognized by the 5D2 antibody, within residues 396-405. Ala400 is the critical amino acid residue conferring epitope specificity. This knowledge confirms that the C-terminal domain of LPL plays a critical role in LPL activity and also provides important information for studies exploring the structure-function relationship of LPL using this antibody.Entities:
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Year: 1992 PMID: 1382603 DOI: 10.1016/0005-2760(92)90264-v
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002