Structure of Somatostatin Isolated from Bovine Retina

Abstract: Somatostatin‐like immunoreactivity (SLI) from bovine retina was purified and its structure determined. Retinal tissue (1868 g) extracted with 3% acetic acid yielded 18.6 nmol SLI. This peptide was purified by chromatography on an affinity column made with anti‐somatostatin antiserum, a reverse‐phase C‐18 HPLC column, and three sequential applications on a reverse‐phase phenyl HPLC column. The peptide was purified 103,000‐fold from the initial extract with an overall yield of 14.4%. Amino acid sequence determination by an automatic Edman degradation technique revealed the sequence to be as follows: Ser ‐ Ala ‐ Asn ‐ Ser ‐ Asn ‐ Pro ‐ Ala ‐ Met ‐ Ala ‐ Pro ‐ Arg ‐ Glu ‐ Arg ‐ Lys ‐ Ala ‐ Gly ‐ (Cys) ‐ Lys ‐ Asn ‐ Phe ‐ Phe ‐ Trp ‐ Lys ‐ Thr ‐ (Phe, Thr, Ser, Cys). The apparent identity of this peptide with somatostatin octacosapeptide (S28) purified from other mammalian tissue indicates the phylogenetic conservation of its structure and facilitates the use of the retina as a model system for studying the neurotransmitter function of somatostatin.

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