• P Nath

      Articles written in Journal of Biosciences

    • Mitochondrial ATP synthase genes may be implicated in cytoplasmic male sterility inSorghum bicolor

      A P Sane P Nath P V Sane

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      Incompatible nuclear-cytoplasmic interactions are responsible for the phenomenon of cytoplasmic male sterility in plants. We have analysed male sterile (2077A, 296A), maintainer fertile (2077B, 296B) and fertility restored (2077R, 296R) lines of sorghum for the restriction fragment locations of various mitochondrial genes and their transcripts. We report here a polymorphism in genes related to the ATP synthase complex between two different cytoplasms from the A and B set of lines of 2077 and 296. There is also a difference in the transcript size of theatpA gene between the A and B cytoplasms. We propose that incompatibility in nuclear cytoplasmic interactions may be explained in terms of incompatible subunits being synthesized by the mitochondria and nucleus for a multisubunit complex of the mitochondrial membrane such as ATPase.

    • Isolation and identification of yolk proteins in Indian major carp,Labeo rohita

      M Bhakta P Nath

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      Two yolk proteins (YP1 and YP2) from the ovaries of Indian major carp, Labeo rohita were isolated by gel filtration and partially characterized by the use of hydroxyapatite ultrogel column in conjunction with native PAGE. On native PAGE YP1 gave a single protein band, whereas YP2 of gel filtration revealed the contamination of YP1, which was removed by adsorption chromatography on hydroxyapatite ultrogel and then the YP2 was the purified one as judged by electrophoresis. Both YP1 and YP2 also stained for lipid and contained alkalilabile phosphorus. Therefore, both yolk proteins were lipophosphoprotein. The molecular weights of YP1 and YP2 were 620 kDa and 225 kDa respectively as determined by gel filtration on Sepharose 4B. When YP1 and YP2 were compared in relation to some physicochemical characteristics with yolk proteins of other oviparous vertebrates including fish, they were lipovitellin like.

      Antiserum to YP2 crossreacted with YP2 and vitellogenin suggesting that YP2 was the cleaved product of vitellogenin. Anti-YP2 antiserum was not crossreacted with native YP1, whereas reduced and/or denatured YP1 was crossreacted indicating the presence of antigenic determinants in the inner core region of YP1 polypeptide.

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