Primary structure analysis proves that protein phosphatases 2C1 and 2C2 are isozymes

Clare H. McGowan; David G. Campbell; Philip Cohen

doi:10.1016/0167-4889(87)90041-3

Primary structure analysis proves that protein phosphatases 2C₁ and 2C₂ are isozymes

Clare H. McGowan, David G. Campbell, Philip Cohen

MRC PPU

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25 Citations (Scopus)

Abstract

The two recently discovered forms of protein phosphatase 2C, termed 2C₁ and 2C₂, were digested with CNBr or trypsin, and several peptides corresponding to two regions of the protein were sequenced. These studies revealed close homology between the two enzymes with 49 identities over the 62 residues that could be compared directly. The results establish that protein phosphatases 2C₁ and 2C₂ are the products of different genes. The C-terminus of protein phosphatase 2C₂ has also been identified.

Original language	English
Pages (from-to)	279-282
Number of pages	4
Journal	BBA - Molecular Cell Research
Volume	930
Issue number	2
DOIs	https://doi.org/10.1016/0167-4889(87)90041-3
Publication status	Published - 14 Sept 1987

Keywords

Amino acid sequence
Protein phosphatase

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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Cite this

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abstract = "The two recently discovered forms of protein phosphatase 2C, termed 2C1 and 2C2, were digested with CNBr or trypsin, and several peptides corresponding to two regions of the protein were sequenced. These studies revealed close homology between the two enzymes with 49 identities over the 62 residues that could be compared directly. The results establish that protein phosphatases 2C1 and 2C2 are the products of different genes. The C-terminus of protein phosphatase 2C2 has also been identified.",

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