scholarly journals Detection of cis-trans Isomers of a Synthetic Peptide Fragment of Erythropoietin

2002 ◽  
Vol 40 (1) ◽  
pp. 1-13 ◽  
Author(s):  
R. D. Husain ◽  
J. McCandless ◽  
P. J. Stevenson ◽  
T. Large ◽  
D. J. S. Guthrie ◽  
...  
Keyword(s):  
Synthetic Peptide ◽  
Peptide Fragment ◽  
Trans Isomers ◽  
Synthetic Peptide Fragment

Expression of the proto-oncogene fos (c-fos) by preimplantation blastocysts of the pig

Development ◽  
1989 ◽  
Vol 105 (3) ◽  
pp. 651-656
Author(s):  
A. Whyte ◽  
H.J. Stewart
Keyword(s):  
Synthetic Peptide ◽  
Expression Vector ◽  
Monolayer Culture ◽  
Peptide Fragment ◽  
Blastocyst Development ◽  
Thin Sections ◽  
Fos Protein ◽  
Rna Probes ◽  
Synthetic Peptide Fragment

Blastocyst material was obtained from 25 pigs during the period 10 to 33 days post coitum, and fixed thin sections of tissue were hybridized in situ to sense and antisense fos RNA probes synthesized using the expression vector Bluescribe M13. Indirect immunofluorescence using antisera to a synthetic peptide fragment of c-fos was used to confirm the tissue distribution of oncogene-encoded proteins, which were shown by immunoprecipitation to have Mrs of 55,000 and 40,000, which are the known Mrs of the fos gene product and an associated nucleoprotein, respectively. Northern and slot blots were used to assess the distribution of c-fos mRNA and the size of the fos transcript was found to be 2.3 kbases. C-fos was expressed in trophectoderm from blastocysts early in pregnancy but declined with increasing blastocyst development so that it was virtually absent by day 19 of gestation. High levels of fos proto-oncogene expression were, however, retained in the allantoic membranes up to at least day 19 of pregnancy. The expression of the fos protein could be prolonged in trophectodermal cells in monolayer culture by addition of conditioned medium from blastocysts cultured for 2 h, suggesting the presence of a growth-factor-like substance.

scholarly journals Chemical studies on histone acetylation using a synthetic peptide fragment of histone H4

FEBS Letters ◽  
1979 ◽  
Vol 98 (1) ◽  
pp. 152-156 ◽  
Author(s):  
Aline Kervabon ◽  
Joseph Parello ◽  
Jean Mery
Keyword(s):  
Histone Acetylation ◽  
Synthetic Peptide ◽  
Peptide Fragment ◽  
Histone H4 ◽  
Synthetic Peptide Fragment ◽  
Chemical Studies

scholarly journals Inhibition of Angiotensin - Converting Enzyme by a Synthetic Peptide Fragment of Glyceraldehyde-3-phosphate Dehydrogenase

2000 ◽  
Vol 55 (7-8) ◽  
pp. 657-660
Author(s):  
Ewa Seweryn ◽  
Artur Pędyczak ◽  
Teresa Banaś
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Angiotensin Converting Enzyme ◽  
Synthetic Peptide ◽  
Human Muscle ◽  
Converting Enzyme ◽  
Peptide Fragment ◽  
Rabbit Lung ◽  
Synthetic Peptide Fragment

Abstract A novel inhibitor of angiotensin - converting enzyme (ACE) identical to a sequence part of human muscle glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was chemically synthesized. Amino acid sequence was as follows Pro - Glu - Asn - Ile - Lys - Trp - Gly - Asp. This peptide inhibited rabbit lung ACE with a K1 value of 1.6 μм. The inhibitor of ACE acts in a non-competitive manner. The amino acid sequence of the new inhibitor was com- pared of GAPDH from other sources.

Atriopeptin II relaxes and elevates cGMP in bovine pulmonary artery but not vein

1986 ◽  
Vol 60 (4) ◽  
pp. 1128-1133 ◽  
Author(s):  
L. J. Ignarro ◽  
K. S. Wood ◽  
R. G. Harbison ◽  
P. J. Kadowitz
Keyword(s):  
Methylene Blue ◽  
Guanylate Cyclase ◽  
Synthetic Peptide ◽  
Soluble Guanylate Cyclase ◽  
Soluble Form ◽  
Peptide Fragment ◽  
Cyclic Monophosphate ◽  
Arterial Relaxation ◽  
Muscle Receptors ◽  
Synthetic Peptide Fragment

Atriopeptin II, a 23-amino acid synthetic peptide fragment of atrial natriuretic factor, caused an endothelium-independent relaxation of isolated precontracted rings of bovine intrapulmonary artery that was accompanied by the concomitant accumulation of guanosine 3′,5′-cyclic monophosphate (cGMP) but not adenosine 3′,5′-cyclic monophosphate. In contrast, rings of intrapulmonary vein were unaffected by atriopeptin II whether or not endothelium was present. Whereas methylene blue, an inhibitor of soluble guanylate cyclase, abolishes endothelium-dependent and independent arterial relaxation and cGMP accumulation in response to acetylcholine and glyceryl trinitrate, respectively, methylene blue failed to alter these responses to atriopeptin II. Similarly, the effects of atriopeptin II were unaltered by propranolol, indomethacin, or atropine. These results indicate that relaxation elicited by atriopeptin II may be selective for arterial smooth muscle receptors, does not require endothelial cells, and does not involve the soluble form of guanylate cyclase, although cGMP accumulation is stimulated.

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