Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.

Search of the DNA sequence data bas revealed a strong homology with the major intrinsic protein of bovine lens, which is the prototype of an ancient but recently recognized family of membrane channels

G. M. Preston; P. Agre

2006

Scholarcy highlights

  • Search of the DNA sequence data bas revealed a strong homology with the major intrinsic protein of bovine lens, which is the prototype of an ancient but recently recognized family of membrane channels
  • The 28-kDa protein behaves as a tetramer when solubilized in Triton X-100, and the N-terminal amino acid sequence of the purified 28-kDa protein is related to that of MIP26, the 26-kDa major intrinsic protein of bovine lens fiber cells
  • The probe used to isolate the channel-like integral membrane protein of 28 kDa cDNA was prepared by a three-step polymerase chain reaction amplification of human fetal liver DNA template
  • The fetal liver PCR products were subcloned into Bluescript vectors. pPCR-3 was used as a probe to isolate a single positive plaque from 250,000 phage in a AgtlO adult human bone marrow cDNA library
  • RNA isolated from mouse kidney contained a similar transcript, suggesting that the red cell and renal tubule CHIP28 proteins may be encoded by the same gene
  • The deduced amino acid sequences of the tandem repeats for channel-like integral membrane protein of 28 kDa and the repeats in seven members of the MIP channel family were compared, and

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