| Literature DB >> 1996958 |
N J Simpkin1, S E Harding, M P Tombs.
Abstract
1. The size of two bacterial lipases was studied by SDS/PAGE, sedimentation velocity and sedimentation equilibrium to test for possible self-association behaviour. 2. Mr values of selected lipases were obtained from SDS/PAGE and sedimentation-velocity measurements, together with an absolute determination by sedimentation equilibrium 3. The Mr values obtained in a variety of aqueous solvents indicate that lipases do not self-associate in solution, suggesting the absence of surface hydrophobic patches.Entities:
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Year: 1991 PMID: 1996958 PMCID: PMC1149807 DOI: 10.1042/bj2730611
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857