Binding of hyaluronan to lysozyme at various pHs and salt concentrations

Binding of hyaluronan to lysozyme at various pHs and salt concentrations

Binding of hyaluronan (HA) to lysozyme immobilized on Sepharose-6B was investigated as a function of pH and NaCl concentration. High affinity binding (Kd = 1.0-2.0 x 10(-8) M) was observed at pH 7.5 and at 10-50 mM NaCl; the number of moles of HA bound to lysozyme was twice as high at 30 mM NaCl as...

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Bibliographic Details
Published in:Biochemistry international Vol. 24; no. 4; p. 605
Main Authors: Van Damme, M P, Moss, J M, Murphy, W H, Preston, B N
Format: Journal Article
Language:English
Published: Australia 01-07-1991
Subjects:
Animals
Cattle
Hyaluronic Acid - metabolism
Hydrogen-Ion Concentration
Muramidase - metabolism
Osmolar Concentration
Sodium Chloride - pharmacology
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Summary:Binding of hyaluronan (HA) to lysozyme immobilized on Sepharose-6B was investigated as a function of pH and NaCl concentration. High affinity binding (Kd = 1.0-2.0 x 10(-8) M) was observed at pH 7.5 and at 10-50 mM NaCl; the number of moles of HA bound to lysozyme was twice as high at 30 mM NaCl as at 10 mM. No specific binding was observed at and above 100 mM NaCl. Binding was suppressed in the presence of chaotropic agents such as guanidinium chloride and urea. These results suggest that binding between HA and lysozyme can occur in the extracellular matrix where an electrolyte concentration as low as 50 mM could be expected due to ionic exclusion by the highly negative charge concentration arising from the polyanions present.
ISSN:0158-5231