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Electrophoretic study of potato tuber plasmalemmal proteins

, : Electrophoretic study of potato tuber plasmalemmal proteins. Biokhimiya 45(9): 1619-1629

The number and qualitative content of proteins extracted from potato tuber plasmalemma by buffer solutions of various ionic strengths and the non-ionic detergent Triton X-100 were investigated. Treatment with the buffer solutions of various ionic strengths results in separation of various amounts of proteins from the membranes. The proteins extracted at various ionic strengths differ in their electrophoretic mobility and the lipo- and glycoprotein sets. The extraction of the bulk of peripheral proteins by buffer solutions does not affect the vesicular structure and the 3-layer structure of the vesicles in the plasmalemmal preparation. Triton X-100 has a destructive effect on the plasmalemma vesicles. The amount of protein extracted with Triton X-100 is relatively low and does not increase with the increase in the detergent concentration from 1% up to 10%. Pretreatment of the preparation with buffer solutions decreases the amount of protein extracted by Triton X-100 irrespective of the ionic strength of the buffer. The electrophoregrams of the proteins extracted by the buffer solutions and Triton X-100 revealed that the detergent can dissolve both structural and peripheral proteins of the plasmalemma. Treatment of plasmalemma with buffer solutions causes separation of hydrophyllic proteins from the membranes and brings about changes in the properties of the membrane-bound proteins.

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