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XB-ART-24297
Arch Biochem Biophys 1991 Dec 01;2912:395-400. doi: 10.1016/0003-9861(91)90152-9.
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Primary structure of the two variants of Xenopus laevis mtSSB, a mitochondrial DNA binding protein.

Ghrir R , Lecaer JP , Dufresne C , Gueride M .


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The primary structure of the single-stranded DNA binding protein from Xenopus laevis oocyte mitochondria (mtSSB) has been determined by Edman degradation of the intact molecule and peptides derived from partial alpha-chymotrypsin proteolysis and enzymatic cleavage with trypsin and endoproteinase Glu-C. The native mtSSB is composed of two related polypeptide chains, mtSSBs and mtSSBr. The sequence of mtSSBs consists of 129 amino acids with a calculated molecular mass of 14,627 Da. Comparison of the first 80 residues of the two chains reveals 91% identity. A high degree of similarity is found between mtSSB and Escherichia coli SSB or F sex factor SSB.

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Species referenced: Xenopus laevis
Genes referenced: prss1 ssb ssbp1