Anantha Samy, TS (1967) Chemical modification of sheep plasma glycoprotein. In: International Journal of Engineering Science, 121 (3). pp. 703-710.
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Glycoprotein isolated from sheep plasma was chemically modified, and the effect of chemical modification on biological activities and immunological cross reactions has been studied. The removal of sialic acid resulted in a change in the “overall conformation” of the glycoprotein as evidenced by a decrease in viscosity of the glycoprotein solution and an increased susceptibility of the glycoprotein to proteolytic enzymes. Sialic acid-free glycoprotein no longer inhibited the tryptic activity or prolonged the clotting time of plasma. However, it could react with the antiserum to sheep plasma glycoprotein. The periodate oxidation of sheep plasma glycoprotein resulted in a complete loss of inhibition of trypsin activity, prolongation of plasma clotting time, and the ability to cross-react with the rabbit antiserum. The significance of periodate oxidation in relation to the possible sequence of sugars in the carbohydrate prosthetic group in the glycoprotein is discussed. Iodination and heating in buffers of acid and alkaline pH values of sheep plasma glycoprotein resulted in complete loss of trypsin activity and ability to prolong plasma clotting time. Iodination of the glycoprotein did not affect the immunological cross-reactivity.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier Science.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||17 May 2010 05:55|
|Last Modified:||19 Sep 2010 06:06|
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