• 제목/요약/키워드: sexual differientiation

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이담자 효모의 세포간 성응집의 특성과 표면단백질의 관련성 (Characterization of Sexual Agglutination and Involvement of Cell-Surface Protein Sexual Cell-Cell Interatrions of Heterobasidiomycetous Yeast)

  • 정영기;이태호;최용락;강원대
    • 한국미생물·생명공학회지
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    • 제23권3호
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    • pp.249-254
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    • 1995
  • When mating type A and a cells of heterobasidiomycetous yeast Rhodosporidium toruloides were mix-cultured, both of the mating type cells have shown strong agglutination. But this agglutination was not detactable when the A and a cell were cultured separately. From reagglutination made just after the result of disassembling the agglutination by sonication, we knew that the agglutination was sexual-agglutination, not simple physical cell agglutination. The sexual agglutination was progressed actively on logarithmic phase and, in addition, progressed faster on mating type a cell treated with rhodotorucine A. These sexual agglutination have been inhibited by several protease such as trypsin, pronase, chymotrpysin and thermolysin and inhibited by 5 mM DTT as well.

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이담자 효모균의 성분화과정에서 막단백질 중 $\Ca^{2+}$-ATPase와 trigger peptidase(TPase)의 상호관계 (Relation of $\Ca^{2+}$-ATPase and trigger peptidase(TPase) that are Membrane Proteins in a Differentiation Process on Heterobasidiomycerous Yeast)

  • 정영기;이태호;정경태
    • 한국미생물·생명공학회지
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    • 제22권1호
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    • pp.1-6
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    • 1994
  • We have studied the relation between Ca$^{2+}$-ATPase and trigger peptidase(TPase) which are membeane protein well known as their significant role for signal transduction of mating pheromone in heterobasidiomycetous yeast. Rhodosporidium toruloides. We found out that there were Ca $^{2+}$-ATPase and TPase together in isolated calmodulim binding protein(CBP), usion calmodulin affinity column chromatography after solubilization of mation type a cell membrane protein, and that the dependence of enzyme activity of both the enzymes on Ca$^{2+}$, phospholipid and nonionic detergent are similar. However, Ca$^{2+}$-ATPase hed quite absolute dependence on calmodulin and, on the other hand, TPase didn't have any dependence. Judging from the fact that there are both enzymes in CBP which the dependence of calmodulin are quite different, we found out that both enzymes were made to their compound and existed in mating type a cell membrane.

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