Subunit analysis of latent and non-latent F1-ATPase from Micrococcus lysodeikticus (luteus).
Limited trypsin and chymotrypsin digestions were performed on the latent F1-ATPase from M. lysodeikticus, and subsequent analysis on SDS-polyacrylamide gels revealed subunit profiles with degraded alpha and delta subunits similar to those of ATPase preparations with spontaneously occurring lower degrees of latency. The ATPase obtained from M. lysodeikticus membranes after n-butanol extraction was also non-latent with similar SDS-gel patterns to the aforementioned ATPases. In addition, the sensitive technique of crossed immunoelectrophoresis was used to show that all of the above ATPases contained alpha, beta, gamma, delta and epsilon subunits but some of them were in degraded forms. Although the delta subunit was the first to be cleaved, the loss of latency can be attributed to the degradation of the alpha subunit.
Urban
C
C
Salton
M R
MR
D000440:Butanols; D002918:Chymotrypsin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007123:Immunoelectrophoresis, Two-Dimensional; D008837:Micrococcus / Q000201:enzymology*; D006180:Proton-Translocating ATPases / Q000032:analysis*; D014357:Trypsin / Q000378:metabolism
D000440:Butanols; D002918:Chymotrypsin; D014357:Trypsin; D006180:Proton-Translocating ATPases