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The main adenosine triphosphate‐binding component of amphibian oocytes is ferritin
Author(s) -
Kandror Konstantin V.,
Stepanov Aleksandr S.,
Tsuprun Vladimir L.
Publication year - 1992
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.1080310109
Subject(s) - biology , adenosine triphosphate , gtp' , guanosine , xenopus , guanosine triphosphate , biochemistry , ferritin , nucleotide , mitochondrion , adenosine , microbiology and biotechnology , enzyme , gene
After fractionation of mitochondrion‐free extracts of Xenopus laevis and Rana temporaria oocytes in sucrose gradients, a distinct peak of adenosine triphosphate (ATP)/guanosine triphosphate (GTP)‐binding activity in the 50–70 S range has been detected. This substance has a boyant density in Cs 2 SO 4 of 1.45 g/cm 3 . The nucleotide‐binding substance has been purified to apparent homogenety. By means of electron microscopy, sodium dodecyl sulfate‐electrophoresis and other methods it has been identified as ferritin.