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Biomedical subjects

D M Peach

Publications and source records attributed to D M Peach.

3 recordsLinked to original sources
PubMed1978

Aggregation of binding protein from rat nerve.

Leucine-binding protein described in an earlier paper was examined to characterize the dynamic properties of the system. Leucine-binding protein assembles into a large protein polymer or complex (greater than 302,000 daltons). Colchicine reduces and Mg2+ increases the amount of polymer formed. Trypsin destroys the isolated polymer but RNAase and collagenase do not. Mg2+-ATPase activity is present in the polymer fraction. The formation of the large complex suggests a quickly adaptable structure capable of responding to ionic and environmental conditions.

Animals↗
PubMed1977

A binding protein from rat nerve.

Leucine has been found to bind competitively to a soluble protein (molecular weight 97,000 daltons) from rat sciatic nerve under certain experimental conditions to form a high molecular weight aggregate (MW greater than 302,000). Kinetic study showed that the equilibrium constant for leucine-binding is 1.33 X 10(4) l/m and the rate constants for binding and unbinding are k1 = 0.424 l/m/sec and k-1 = 3.18 X 10(5) sec-1 respectively. The binding reaction is accompanied by an endothermic enthalpy change of 5,000 cal/mole and the favorable equilibrium appears to be due to the large positive (35.3 eu) entropy of binding. L-Proline, thymidine, and succinic acid were also found to bind, non-competitively with leucine, to proteins in the same fraction. Binding of those compounds and leucine was enhanced by the presence of Mg2+. Rat muscle and plasma proteins did not significantly bind leucine under these experimental conditions. The presence of this binding protein in rat nerve suggests an additional mechanism in the metabolism and in the transport of amino acids for incorporation into a protein structure in nerve.

Animals↗