c-peptide and eristostatin

c-peptide has been researched along with eristostatin* in 1 studies

Other Studies

1 other study(ies) available for c-peptide and eristostatin

Article	Year
Inhibition of platelet aggregation of a mutant proinsulin molecule engineered by introduction of a native Arg-Gly-Asp sequence. Applied biochemistry and biotechnology, 2001, Volume: 90, Issue:1 A 13 amino acid sequence, CRVARGDWNDNYC, originated from disintegrin eristostatin, was introduced into an inactive human proinsulin molecule between the B29 and A2 sites to replace proinsulin C-peptide by molecular cloning techniques. The constructed Arg-Gly-Asp (RGD)-proinsulin gene was cloned into a temperature-inducible vector pBV220 and expressed in Escherichia coli. The expressed RGD-proinsulin was refolded and purified by Sephadex G50 and DEAE-Sephadex A25 separations. The chemical identity was confirmed by both amino acid composition and mass spectrometry analyses. This RGD-proinsulin showed an inhibitory activity of adenosine 5'-diphosphate-induced human platelet aggregation with an IC50 value of 200 nM. Its insulin receptor binding activity remained as low as 0.03% with native insulin as a control, and its insulin immune activity retained 27.6% compared with proinsulin. Topics: Adenosine Diphosphate; Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; C-Peptide; Circular Dichroism; Disintegrins; Escherichia coli; Humans; Inhibitory Concentration 50; Insulin; Mass Spectrometry; Models, Molecular; Mutagenesis, Insertional; Oligopeptides; Peptides; Platelet Aggregation; Proinsulin; Protein Engineering; Protein Renaturation; Protein Structure, Secondary; Receptor, Insulin; Recombinant Fusion Proteins; Viper Venoms	2001

Article

Year

Inhibition of platelet aggregation of a mutant proinsulin molecule engineered by introduction of a native Arg-Gly-Asp sequence.

Applied biochemistry and biotechnology, 2001, Volume: 90, Issue:1

A 13 amino acid sequence, CRVARGDWNDNYC, originated from disintegrin eristostatin, was introduced into an inactive human proinsulin molecule between the B29 and A2 sites to replace proinsulin C-peptide by molecular cloning techniques. The constructed Arg-Gly-Asp (RGD)-proinsulin gene was cloned into a temperature-inducible vector pBV220 and expressed in Escherichia coli. The expressed RGD-proinsulin was refolded and purified by Sephadex G50 and DEAE-Sephadex A25 separations. The chemical identity was confirmed by both amino acid composition and mass spectrometry analyses. This RGD-proinsulin showed an inhibitory activity of adenosine 5'-diphosphate-induced human platelet aggregation with an IC50 value of 200 nM. Its insulin receptor binding activity remained as low as 0.03% with native insulin as a control, and its insulin immune activity retained 27.6% compared with proinsulin.

Topics: Adenosine Diphosphate; Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; C-Peptide; Circular Dichroism; Disintegrins; Escherichia coli; Humans; Inhibitory Concentration 50; Insulin; Mass Spectrometry; Models, Molecular; Mutagenesis, Insertional; Oligopeptides; Peptides; Platelet Aggregation; Proinsulin; Protein Engineering; Protein Renaturation; Protein Structure, Secondary; Receptor, Insulin; Recombinant Fusion Proteins; Viper Venoms

2001