Detail of "837-83-2"

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Conformons in amino acid sequences typical of collagen: a quantum mechanical study

Conformons in amino acid sequences typical of collagen: a quantum mechanical study. Vasilescu, D.; Cabrol, D.; Broch, H. (Biophys. Lab., Univ. Nice, Fr.). Int. J. Quantum Chem., Quantum Biol. Symp., 10, 109-22 (English) 1983. CODEN: IJQBDZ. ISSN: 0360-8832. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) A systematic conformational anal. study of the tripeptidic units (Gly-X-Pro) and (Gly-Pro-X), with X = Pro, Ala, Ser, Val, Leu, Ile, and Phe, are reported. Conformations of each X residue were studied with the PCILO method. The amino acid side chain conformations were detd. with the main chain fixed in 2 selected forms: d collagen helix and extended conformation Z [c1,c2) space]. The backbone flexibility was studied with regard to various conformations of the amino acid side chain [(f,y) space]. Thus, one may define an amino acid local conformon by combining specific regions of the (f,y) maps (i.e., d collagen helix; Ra, La, and g helixes; b sheets) with preferential orientations of the side chains (G+, T, and G-). The results are presented on the basis of ~180 isoenergetic maps in the (f,y) or (c1,c2) space. The low-energy conformons obtained by these quantum computations are discussed with respect to other theor. investigations or exptl. protein structures. For all the studied residues, it was obsd. that the R3 location induces more conformons than the R2 location; the R2 location implies the impossibility of access to the local Ra conformation.Except for chemicals metioned above, 23828-66-2 and 837-83-2 are also used. In the R2 location, for each residue a preferred side chain conformation is obtained, independently of the backbone conformation for this residue. .

Partial purification and characterization of an ovarian tripeptidyl peptidase: a lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets

Partial purification and characterization of an ovarian tripeptidyl peptidase: a lysosomal exopeptidase that sequentially releases collagen-related (Gly-Pro-X) triplets. McDonald, J. Ken; Hoisington, Anne R.; Eisenhauer, Donald A. (Dep. Biochem., Med. Univ. South Carolina, Charleston, SC 29425, USA). Biochem. Biophys. Res. Commun., 126(1), 63-71 (English) 1985. CODEN: BBRCA9. ISSN: 0006-291X. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The pregnant hog ovary is a rich source of a novel exopeptidase that catalyzes the release, at pH 5.0, of collagen-related (P3-P2-P1) triplets such as Gly-Pro-Met, Gly-Pro-Arg, and Gly-Pro-Ala from arylamide derivs., provided the N-terminal ends are unsubstituted. Corresponding derivs. of related (P2-P1) dipeptides (Pro-Met, Pro-Ala) or (P1) amino acids (Met, Arg, Ala) are not attacked. The enzyme was purified 58-fold from a detergent ext. of a H2O-extd. tissue residue. Activity was detd. 837-83-2 is also in the experiment. on Gly-Pro-Met-2-naphthylamide at pH 4.5 and 37° (Km 0.45 mM; Vmax 722 nmoles/min/mg protein). The responsible mol. wt. (Mr 55,000 exopeptidase, termed tripeptidyl peptidase, forms high-Mr aggregates, belongs to the serine catalytic class, and has a lysosomal localization. Gly-Pro-Ala triplets were released sequentially at pH 5. There are some commonly used reagents like 837-83-2 in this article.0 from a Mr 14,000 polypeptide, poly(Gly-Pro-Ala-). When this reaction was coupled to that of homologous dipeptidase II, the liberated tripeptides were reduced to dipeptides and free amino acids: (Gly-Pro-Ala)n ? nGly-Pro-Ala ? nGly-Pro + nAla. ..