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CLIV is a multiple antigen peptide ([PTKAKRRVVQREKR] 4 -K 2 -K-βA) that encompasses the cleavage region of the human immunodeficiency virus type 1 (HIV-1) envelope precursor. It displays an antiviral activity against HIV-1 and HIV-2 and inhibits HIV-1 Env-mediated cell-to-cell fusion. This effect has previously been attributed to interference with Env processing, resulting in the expression...
SPC 3 is a multiple antigen peptide derived from the V 3 loop of human immunodeficiency virus (HIV) envelope (Env). It exerts a potent anti-HIV activity whereas it alters neither Env expression nor binding to CD 4 . Here, SPC 3 binding characteristics, its subsequent intracellular fate and the fact that it inhibited SDF 1 α binding to the lymphocyte surface...
A 22-amino-acid-long multibranched peptide construct (CLV) derived from the cleavage region (KIEPLGVAPTKAKRR*VVQREKR*) of the human immunodeficiency virus (HIV) type-1 envelope precursor inhibits HIV infection (Virology,1996, 223, 406–408). We attempted to characterize its activity for Env expressedviaa recombinant vaccinia virus (rVV): gp160 cleavage was delayed, but not impaired, in the presence...
Cerastocytin is a thrombin-like serine protease with potent platelet-proaggregating properties. It is able to activate factor XIII but is less active than thrombin on plasma coagulation. The aggregation induced by cerastocytin ressembles that induced by thrombin, since rabbit washed platelets desensitized by a pretreatment with thrombin do not aggregate in the presence of cerastocytin. Furthermore,...
Cerastatin, a potent platelet aggregation inhibitor, was purified by gel filtration on Sephadex G-75, followed by two ion exchange chromatographies on Mono-S columns. Cerastatin is a neutral glycoprotein (pI = 6.2) of 32 kDa, made up of at least three subunits. It is devoid of phospholipase A 2 , esterase, fibrinogenolytic and amidolytic activities. It inhibits aggregation of washed platelets,...
Lebetins 1 and Lebetins 2, two polypeptide groups that inhibit platelet aggregation, were isolated from Vipera lebetina venom by gel filtration and reverse phase chromatography. Amino acid sequencing indicated that the first group contains two major polypeptides of 13 and 12 residues; their molecular weight was determined by electrospray mass spectrometry. The second was composed of two peptides...
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