Literature DB >> 131581

Me2+-(13 S) ATPase from Micrococcus sp. ATCC 398E. The effect of trypsin on the purified enzyme.

M Höckel, F W Hulla, S Risi, K Dose.   

Abstract

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.

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Year:  1976        PMID： 131581     DOI： 10.1016/0005-2744(76)90346-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  3 in total

Review 1.  Structure and function of H+-ATPase.

Authors:  Y Kagawa; N Sone; H Hirata; M Yoshida
Journal:  J Bioenerg Biomembr       Date:  1979-08       Impact factor: 2.945

2.  Role of the subunits of the energy-transducing adenosine triphosphatase from Micrococcus lysodeikticus membranes studied by proteolytic digestion and immunological approaches.

Authors:  F Mollinedo; V Larraga; F J Coll; E Muñoz
Journal:  Biochem J       Date:  1980-03-15       Impact factor: 3.857

3.  Reconstitution of thermostable ATPase capable of energy coupling from its purified subunits.

Authors:  M Yoshida; H Okamoto; N Sone; H Hirata; Y Kagawa
Journal:  Proc Natl Acad Sci U S A       Date:  1977-03       Impact factor: 11.205
  3 in total

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