期刊
BIOPHYSICAL JOURNAL
卷 81, 期 4, 页码 2370-2377出版社
BIOPHYSICAL SOCIETY
DOI: 10.1016/S0006-3495(01)75883-3
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资金
- NIAMS NIH HHS [R01 AR39472, R01 AR40618] Funding Source: Medline
- NIGMS NIH HHS [R01 GM38838] Funding Source: Medline
An investigation of gelatinase A binding to gelatin produced results that are inconsistent with a traditional bimolecular Michaelis-Menten formalism but are effectively accounted for by a power law characteristic of fractal kinetics. The main reason for this inconsistency is that the bulk of the gelatinase A binding depends on its ability to diffuse laterally on the gelatin surface. Most interestingly, we show that the anomalous lateral diffusion and, consequently, the binding to gelatin is greatly facilitated by the C-terminal hemopexin-like domain of the enzyme whereas the specificity of binding resides with the fibronectin-like gelatin-binding domain.
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