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Purification of a putative brain somatostatin receptor

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (USA)
; ; ;  [1]
  1. Univ. of Pennsylvania School of Medicine, Philadelphia (USA)
The brain somatostatin receptor was purified by affinity chromatographic techniques. A protein of 60 kDa could be purified from rat brain. The protein was eluted from a (D-Trp{sup 8})SRIF affinity column with either sodium acetate (pH 5.5) or free (D-Trp{sup 8})SRIF. The binding of the protein to the affinity column was prevented by free (D-Trp{sup 8})SRIF or the stable SRIF analogue SMS 201-996 but not by the inactive somatostatin 28-(1-14). The purified receptor could be covalently labeled by the {sup 125}I-labeled SRIF analogue CGP 23996. Excess (D-Trp{sup 8})SRIF blocked the binding of {sup 125}I-labeled CGP 23996 to the purified receptor, but somatostatin 28-(1-14) did not affect the binding. A 60-kDa protein was also purified from the anterior pituitary cell line AtT-20, which has a high expression of SRIF receptors. In contrast, no 60-kDa protein could be purified from CHO cells, which have no detectable SRIF receptors. These findings present evidence for the purification of the SRIF receptor.
OSTI ID:
5085184
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (USA), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (USA) Vol. 86:5; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English