Detail of "95076-93-0"

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A novel secreted cyclophilin-like protein (SCYLP)

A novel secreted cyclophilin-like protein (SCYLP). Spik, Genevieve; Haendler, Bernard; Delmas, Olivier; Mariller, Christophe; Chamoux, Muriel; Maes, Pierrette; Tartar, Andre; Montreuil, Jean; Stedman, Kenneth; et al.Several substances are used for example 95076-93-0 and 59865-13-3 which are their cas registry numbers. (Lab. Chim. Biol., Univ. Sci. Tech. Lile Flandres-Artois, Villeneuve d'Ascq 59655, Fr.). J. Biol. Chem., 266(17), 10735-8 (English) 1991. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 3, 13 A novel cyclosporin A-binding glycoprotein of 21 kDa was isolated from human milk by several steps of cation-exchange chromatog. The corresponding gene was cloned from human T cells, expressed in Escherichia coli and the recombinant protein purified. The protein shares 58% amino acid identity with the cytosolic cyclophilin and is initially synthesized with a hydrophobic leader sequence. The cyclophilin-like protein also has peptidyl-prolyl cis/trans-isomerase activity, although less efficient, that is inhibited by cyclosporin A. The existence of a secreted form of cyclophilin-like protein in addn. to the previously known cytosolic cyclophilin implies that these proteins act on different in vivo targets. .

Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase

Cis-trans isomerization is rate-determining in the reactivation of denatured human carbonic anhydrase II as evidenced by proline isomerase. Fransson, Cecilia; Freskgaard, Per Ola; Herbertsson, Helena; Johansson, Aasa; Jonasson, Per; Martensson, Lars Goeran; Svensson, Magdalena; Jonsson, Bengt Harald; Carlsson, Uno (Dep. Chem., Linkoeping Univ., Linkoeping S-581 83, Swed.). FEBS Lett., 296(1), 90-4 (English) 1992. CODEN: FEBLAL. ISSN: 0014-5793. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The refolding of human carbonic anhydrase II is a sequential process. The slowest step involved is the recovery of enzymic activity (t1/2 = 9 min). Kinetic data from double-jump measurements indicate that proline isomerization might be rate detg. in the reactivation of the denatured enzyme.Several substances with their cas registry numbers 95076-93-0 and 9001-03-0 may be metioned in this study. Proof of this is provided by the effect of proline isomerase on the reactivation kinetics: the presence of isomerase during reactivation lowers the half-time of the reaction to 4 min, and inhibition of proline isomerase completely abolishes this kinetic effect. A similar acceleration of the refolding process by proline isomerase is also obsd. for bovine carbonic anhydrase II, in contrast to what has previously been reported. In human carbonic anhydrase II there are two cis-peptidyl-Pro bonds at Pro30 and Pro202. Two asparagine single mutants (P30N and P202N) and a glycine double mutant (P30G/P202G) were constructed to investigate the role of these prolines in the rate limitation of the reactivation process. Both in the presence and absence of PPIase the P202N mutant behaved exactly like the unmutated enzyme. Thus, cis-trans isomerization of the Pro202 cis-peptidyl bond is not rate detg. in the reactivity process. The mutations at position 30 led to such extensive destabilization of the protein that the refolding reaction could not be studied. .