The complete amino‐acid sequence of anglerfish somatostatin‐28 II

Morel, Alain; Chang, Jui‐Yoa; Cohen, Paul A.

doi:10.1016/0014-5793(84)80561-x

Cited by 24 publications

(2 citation statements)

References 16 publications

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“…The complete amino acid sequence of the here described somatostatin-28 II was determined (24). The primary structure is in total agreement with the one predicted from cDNA sequencing (7).…”

Section: Methodssupporting

confidence: 72%

Characterization of a somatostatin-28 containing the (Tyr-7, Gly-10) derivative of somatostatin-14: a terminal active product of prosomatostatin II processing in anglerfish pancreatic islets.

Morel¹,

Gluschankof²,

Gomez³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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Anglerfish (Lophius piscatorius) Brockmann organs contain a form of somatostatin-14, identical to the hypothalamic tetradecapeptide, and two distinct forms of somatostatin-28, which can be separated by reversed-phase highpressure liquid chromatography (HPLC). Analysis of the NH2-terminal amino acid sequence and comparison of the ability to incorporate 1251 indicate that one of these forms corresponds to an octacosapeptide including in its sequence the (Tyr-7, Gly-10) derivative of somatostatin-14 (somatostatin II). Exposure of this somatostatin-28 species to an endopeptidase activity from the rat brain cortex generates a peptide immunologically related to somatostatin and undistinguishable from synthetic (Tyr-7, Gly-10) somatostatin-14 II by HPLC. This somatostatin-28 II exhibits a potent inhibitory effect on growth hormone release by rat anterior pituitary cells, comparable to the other somatostatin-28 form. Since (Tyr-7, Gly-10) somatostatin-14 II cannot be detected in anglerfish pancreatic islets, these results indicate that somatostatin-28 II represents the terminal active product of prosomatostatin II processing, whose structure was predicted from the cDNA nucleotide sequence corresponding to the second mRNA cloned from ang-

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“…The complete amino acid sequence of the here described somatostatin-28 II was determined (24). The primary structure is in total agreement with the one predicted from cDNA sequencing (7).…”

Section: Methodssupporting

confidence: 72%

Characterization of a somatostatin-28 containing the (Tyr-7, Gly-10) derivative of somatostatin-14: a terminal active product of prosomatostatin II processing in anglerfish pancreatic islets.

Morel¹,

Gluschankof²,

Gomez³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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“…Manual sequencing was carried out using the DABITC (4-N-N dimethylamine benzene-4'-thiocyanate)/PITC (phenylisothiocyanate) method as described by Morel et al (1984).…”

Section: Fapy-dna Glycosylase Assaymentioning

confidence: 99%

Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein.

1987

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An Escherichia coli genomic library composed of large DNA fragments (10‐15 kb) was constructed using the plasmid pBR322 as vector. From it 700 clones were individually screened for increased excision of the ring‐opened form of N7‐methylguanine (2‐6‐diamino‐4‐hydroxy‐5N‐methyl‐formamidopyrimidine) or Fapy. One clone overproduced the Fapy‐DNA glycosylase activity by a factor of 10‐fold as compared with the wild‐type strain. The Fapy‐DNA glycosylase overproducer character was associated with a 15‐kb recombinant plasmid (pFPG10). After subcloning a 1.4‐kb fragment which contained the Fapy‐DNA glycosylase gene (fpg+) was inserted in the plasmids pUC18 and pUC19 yielding pFPG50 and pFPG60 respectively. The cells harbouring pFPG60 displayed a 50‐ to 100‐fold increase in glycosylase activity and overexpressed a 31‐kd protein. From these cells the Fapy‐DNA glycosylase was purified to apparent physical homogeneity as evidenced by a single protein band at 31 kd on SDS‐polyacrylamide gels. The amino acid composition of the protein and the amino acid sequence deduced from the nucleotide sequence demonstrate that the cloned fragment contains the structural gene coding for the Fapy‐DNA glycosylase. The nucleotide sequence of the fpg gene is composed of 809 base pairs and codes for a protein of 269 amino acids with a calculated mol. wt of 30.2 kd.

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Sequences of Natural Gut Peptides, Related Peptides, and Their Precursors

Yanaihara

1989

Comprehensive Physiology

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The complete amino‐acid sequence of anglerfish somatostatin‐28 II

Cited by 24 publications

References 16 publications

Characterization of a somatostatin-28 containing the (Tyr-7, Gly-10) derivative of somatostatin-14: a terminal active product of prosomatostatin II processing in anglerfish pancreatic islets.

Characterization of a somatostatin-28 containing the (Tyr-7, Gly-10) derivative of somatostatin-14: a terminal active product of prosomatostatin II processing in anglerfish pancreatic islets.

Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein.

Sequences of Natural Gut Peptides, Related Peptides, and Their Precursors

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