Identification of a processed protein related to the human chaperonins (hsp 60) protein in mammalian kidney

Willie R. Ross, William S. Bertrand, Aubrey R. Morrison

Research output: Contribution to journalArticlepeer-review

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The chaperonin family of proteins, which includes GroEL protein of E. coli, yeast heat shock protein (hsp-60) and the ribulose-1-5-bisphosphate carboxylase (Rubis Co.) subunit binding protein of plant choloroplasts, shows strong sequence homology to the Chinese hamster ovary (CHO) mitochondrial P1 protein. We have identified a 60 kDa protein from bovine kidney which by N-terminal sequencing gives the amino acid sequence AKDVKFGADARALLMLQGVDLLADA. Bovine whole kidney membranes were delipidated, solubilized with octyl glucoside and fractionated over an affinity column using the amiloride analog 5-N pyrazine amiloride as the ligand. After extensive washing with 200 mM NaCl, the column was eluted with pH 4.0 buffer. Analysis of column fractions on a 7.5% polyacrylamide gel revealed 3-4 bands with a predominant band at 60,000 Da. Amino acid analysis after transfer to immobilon membranes demonstrated sequence identity to the human HSP (60), extending 24 amino acids from the N-terminus, but lacking the leader sequence. These data indicate that a processed form of a protein related to the human HSP (60) chaperonin is associated with a membrane fraction in the mammalian kidney, and that the processed form of the protein binds strongly to an amiloride affinity support.

Original languageEnglish
Pages (from-to)683-687
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
StatePublished - Jun 15 1992


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