A study of the water-soluble proteins of the seeds of the cotton plants Gossypium hirsutum and G. barbadense

It has been shown by electrophoresis in polyacrylamide gel that different enzymes with similar electrophoretic mobilities may be localized in one and the same zone of water-soluble cottonseed proteins. Some zones not stained by the usual protein dyes also possess enzymatic activity. It has been established that the majority of the electrophoretic fractions consist of a series of polypeptides with different molecular weights, mainly of low-molecular-weight nature. The results are given of an investigation of the peroxidase, α-amylase, lipase, NADH-DCPIP oxidoreductase, and NADPH-DCPIP oxidoreductase activities of the water soluble fraction of the proteins of the seeds of the species mentioned.     

Proteins of the seeds ofRicinis communis. I. A study of the water-soluble proteins of the seeds and meal ofRicinis communis

The electrophoretic spectrum of the water-soluble proteins of the seeds and meal of the castor-oil plant has been studied. A correlation has been found between a decrease in the relative amount of electrophoretic components with R_f 0.04 and 0.11 and the hemagglutinating activity of the meal.Institute of the Chemistry of Plant Substances of the Uzbek SSR Academy of Sciences, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 630–631, September–October, 1960.     

Conjugations between circle maps with a single break point

Consider two circle homeomorphisms fi∈C2+α(S?{bi}), α>0, i=1,2 with a single break point bi i.e. a discontinuity in the derivative Dfi, and identical irrational rotation number ρ. Suppose the jump ratios and do not coincide. Then the map ψ conjugating f₁ and f₂ is a singular function i.e. it is continuous on S¹ and Dψ(x)=0 a.e. with respect to Lebesgue measure.     

A study of the water-soluble proteins of the seeds of the cotton plants Gossypium hirsutum and G. barbadense

It has been shown by electrophoresis in polyacrylamide gel that different enzymes with similar electrophoretic mobilities may be localized in one and the same zone of water-soluble cottonseed proteins. Some zones not stained by the usual protein dyes also possess enzymatic activity. It has been established that the majority of the electrophoretic fractions consist of a series of polypeptides with different molecular weights, mainly of low-molecular-weight nature. The results are given of an investigation of the peroxidase, -amylase, lipase, NADH-DCPIP oxidoreductase, and NADPH-DCPIP oxidoreductase activities of the water soluble fraction of the proteins of the seeds of the species mentioned.Institute of Experimental Plant Biology, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 488–491, July–August, 1986.     

Proteins of the seeds ofRicinis communis. I. A study of the water-soluble proteins of the seeds and meal ofRicinis communis

The electrophoretic spectrum of the water-soluble proteins of the seeds and meal of the castor-oil plant has been studied. A correlation has been found between a decrease in the relative amount of electrophoretic components with R_f 0.04 and 0.11 and the hemagglutinating activity of the meal.