Me2+-(13 S) ATPase from Micrococcus sp. ATCC 398E. The effect of trypsin on the purified enzyme.
By trypsin treatment of highly purified ATPase (EC 3.6.1.3) from Micrococcus sp. ATCC 398E, two enzyme modifications have been obtained. (i) ATPase Ta, which has about the same activity as untreated ATPase. (ii) A protein complex Ti, which lacks ATPase activity, but nevertheless binds ATP as shown by affinity chromatography. Trypsin primarily shortens the alpha-chains of the "native" enzyme to alpha-chains and removes the gamma-subunit, thus yielding ATPase Ta. The formation of the protein complex Ti appears to be due to additional cleavage of one alpha-chain into at least two more fractions.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001665:Binding Sites; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D008837:Micrococcus / Q000201:enzymology*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis / Q000378:metabolism; D011485:Protein Binding; D014357:Trypsin / Q000494:pharmacology*
D010446:Peptide Fragments; D014357:Trypsin; D000251:Adenosine Triphosphatases