A comprehensive survey of the acid-stable fluorescent cross-links formed by ribose with basic amino acids, and partial characterization of a novel Maillard cross-link

1996 ◽  
Vol 1297 (1) ◽  
pp. 9-16 ◽  
Author(s):  
Lila Graham
Keyword(s):  
Amino Acids ◽  
Partial Characterization ◽  
Cross Link ◽  
Basic Amino Acids ◽  
Comprehensive Survey ◽  
Cross Links ◽  
Acid Stable

scholarly journals Chemistry of the collagen cross-links. Origin and partial characterization of a putative mature cross-link of collagen

1987 ◽  
Vol 244 (2) ◽  
pp. 303-309 ◽  
Author(s):  
K Barnard ◽  
N D Light ◽  
T J Sims ◽  
A J Bailey
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Partial Characterization ◽  
Cross Link ◽  
Cross Links

The conversion of the reducible divalent cross-links in collagen to non-reducible multivalent cross-links in mature collagen has resulted in the identification of several new amino acids as the putative mature cross-link. None of these compounds has completely satisfied the necessary criteria. We have now isolated an amino acid of high Mr, derived from lysine, that is only present in high-Mr peptides derived from mature collagen. Its increase with age of the tissue correlates with the decrease in the reducible cross-links, and it is present both in mature skin and bone, which are initially cross-linked through the aldimine and oxo-imine divalent cross-link respectively. We propose that this amino acid, as yet incompletely characterized and designated compound M, is a major cross-link of mature collagen.

Isolation and partial characterization of a peptidase with trypsin-like activity from bovine adenohypophysis

1989 ◽  
Vol 54 (8) ◽  
pp. 2276-2286
Author(s):  
Tsezengijn Dash ◽  
Tomislav Barth ◽  
Jiřina Slaninová ◽  
Jana Barthová ◽  
Hana P. Mašková ◽  
...  
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Partial Characterization ◽  
Chromogenic Substrate ◽  
Fluorogenic Substrate ◽  
Basic Amino Acids ◽  
Optimum Ph ◽  
Reproducible Method ◽  
Hydrolysis Of

A reproducible method has been developed for the isolation of the adenohypophyseal enzyme with a trypsin-like activity. The enzyme is able to hydrolyze Nα-benzoyl-L-arginine-p-nitroanilide, a fluorogenic substrate CBzl-Arg-Arg-β-naphthyl amide and some peptides with one or two accumulated basic amino acids in the chain. The optimum pH for hydrolysis of the chromogenic substrate was within the range 6.0-7.0 (Km = 0.66 mmol l-1), in the case of the fluorogenic substrate the range was between 7.0 and 7.5 (Km = 1.2 μmol l-1). The enzyme is activated by cysteine and dithiothreitol and inhibited by SH-poisons. The molecular weight of the enzyme, determined by means of two independent methods, was approximately 25 kDA.

Effects of Aspirin or Basic Amino Acids on Collagen Cross-Links and Complications in NIDDM

Diabetes Care ◽  
1997 ◽  
Vol 20 (5) ◽  
pp. 832-835 ◽  
Author(s):  
I. Contreras ◽  
K. M. Reiser ◽  
N. Martinez ◽  
E. Giansante ◽  
T. Lopez ◽  
...  
Keyword(s):  
Amino Acids ◽  
Basic Amino Acids ◽  
Cross Links

scholarly journals The chemistry of the collagen cross-links. The characterization of Fraction C, a possible artifact produced during the reduction of collagen fibres with borohydride

1973 ◽  
Vol 135 (4) ◽  
pp. 657-665 ◽  
Author(s):  
Simon P. Robins ◽  
Allen J. Bailey
Keyword(s):  
Aldol Condensation ◽  
Condensation Product ◽  
Reduced Form ◽  
Borohydride Reduction ◽  
Cross Link ◽  
Collagen Fibres ◽  
Isolation And Identification ◽  
Cross Links

The present paper describes the isolation and identification of a major radioactive component of borotritide-reduced collagen, previously designated Fraction C. The derived structure for the compound confirms that it is identical with the ‘post-histidine’ component described by Tanzer et al. (1973) and given the trivial name histidino-hydroxymerodesmosine. Detailed studies of the effects of acid pH on the formation of Fraction C after borohydride reduction demonstrated the apparent lability of the non-reduced form, thus confirming our previous findings (Bailey & Lister, 1968). Inhibition of the formation of this component by the acid treatment appears to be due to protonation of the histidine imidazole group. Since the only new component formed on reduction of the acid-treated fibres was the reduced aldol condensation product, these results indicate that neither the histidine nor the hydroxylysine residues can be involved in covalent linkage with the aldol condensation product in the native fibre. It is suggested therefore that the proposed non-reduced aldimine form of Fraction C does not exist as an intermolecular cross-link in vivo. Thus the presence of histidino-hydroxymerodesmosine as a tetrafunctional cross-link in reduced collagen fibres is a result of a base-catalysed reaction promoted by the borohydride-reduction procedure and this component must therefore be considered as an artifact.

PARTIAL CHARACTERIZATION OF SOIL HUMIC ACIDS THROUGH BIODEGRADATION

1967 ◽  
Vol 13 (5) ◽  
pp. 581-586 ◽  
Author(s):  
S. P. Mathur ◽  
E. A. Paul
Keyword(s):  
Amino Acids ◽  
Oxygen Tension ◽  
Humic Acids ◽  
Aromatic Amino Acids ◽  
Partial Characterization ◽  
Penicillium Frequentans ◽  
Enzyme Systems ◽  
Culture Filtrates ◽  
Partial Degradation

A strain of Penicillium frequentans was successfully employed for partial degradation and characterization of humic acids. Salicyl alcohol and salicylaldehyde were detected in culture filtrates of the fungus utilizing humates under reduced oxygen tension. The enzyme systems involved in the degradation of humic acids were adaptive. The humate-adapted mycelium was capable of metabolizing a number of compounds which occur in soil as products of degradation of lignin, aromatic amino acids, and plant glycosides but not polyphenolic hydrocarbons, resorcinol, and phloroglucinol.

scholarly journals Characterization of the yeast KEX1 gene product: a carboxypeptidase involved in processing secreted precursor proteins.

1989 ◽  
Vol 9 (6) ◽  
pp. 2706-2714 ◽  
Author(s):  
A Cooper ◽  
H Bussey
Keyword(s):  
Amino Acids ◽  
Gene Product ◽  
Killer Toxin ◽  
Secreted Protein ◽  
Serine Carboxypeptidase ◽  
Carboxypeptidase B ◽  
Basic Amino Acids ◽  
Precursor Proteins ◽  
In Cells

We have identified and partially characterized the Saccharomyces cerevisiae KEX1 gene product, Kex1p, to assess its role in processing secreted protein precursors. Anti-Kex1p antibodies identified a 113-kilodalton protein that was absent in cells in which the KEX1 gene has been disrupted and that was more abundant in cells overexpressing the KEX1 gene. Kex1p was found to be a membrane-associated glycoprotein with N-linked carbohydrate. The N-linked oligosaccharide(s) was modified in a progressive manner after synthesis, causing the glycoprotein to slowly increase in mass to 115 kilodaltons. After a Kex2p-mediated cleavage event at specific pairs of basic amino acids, alpha-factor and K1 killer toxin precursors have COOH-terminal dibasic residue extensions and require a carboxypeptidase B-like enzyme to process the precursors to maturity. A carboxypeptidase activity, with apparent specificity for basic amino acids, was detected in KEX1 cells. Disruption of the KEX1 gene abolished this activity, while overexpression of KEX1 increased it. Our results provide biochemical evidence consistent with earlier genetic work, that KEX1 encodes a serine carboxypeptidase involved in the processing of precursors to secreted mature proteins.

scholarly journals Preparation and Characterization of Acrylic Hydrogels Neutralized by Basic Amino Acids.

2000 ◽  
Vol 48 (11) ◽  
pp. 1828-1830 ◽  
Author(s):  
Takahiro UCHIDA ◽  
Yuka TOIDA ◽  
Yohko MIYANAGA ◽  
Kotoe MACHIDA ◽  
Koichi WADA ◽  
...  
Keyword(s):  
Amino Acids ◽  
Basic Amino Acids

scholarly journals The chemistry of the collagen cross-links. A convenient synthesis of the reduction products of several collagen cross-links and cross-link precursors

1972 ◽  
Vol 129 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Norman R. Davis ◽  
Allen J. Bailey
Keyword(s):  
Amino Acids ◽  
The Other ◽  
Cross Link ◽  
Unusual Amino Acids ◽  
Convenient Synthesis ◽  
Cross Links ◽  
Synthetic Routes ◽  
Synthetic Intermediate

New synthetic routes to the reduction products of several collagen cross-links and cross-link precursors are described. By the use of these routes hydroxynorleucine, 5,6-dihydroxynorleucine, hydroxylysinonorleucine and hydroxylysinohydroxynorleucine can be synthesized via one common synthetic intermediate. The synthetic routes provide a convenient source of these unusual amino acids, as well as confirming the structure of hydroxylysinohydroxynorleucine and the other lysine-derived residues found in borohydride-reduced collagens.

scholarly journals The chemistry of the collagen cross-links. Purification and characterization of cross-linked polymeric peptide material from mature collagen containing unknown amino acids

1980 ◽  
Vol 185 (2) ◽  
pp. 373-381 ◽  
Author(s):  
N D Light ◽  
A J Bailey
Keyword(s):  
Amino Acids ◽  
Type I Collagen ◽  
Gel Filtration ◽  
Amino Acid Content ◽  
Exchange Chromatography ◽  
Type I ◽  
Polymeric Form ◽  
Cross Links ◽  
Helical Region

A polymeric form of the alpha 1-chain C-terminal peptide alpha 1 CB6 (poly-alpha 1 CB6) was purified from CNBr digests of insoluble bovine tendon type-I-collagen by gel filtration and ion-exchage chromatography. The purified material had a molecular weight of 1.5 × 10(6)-5 × 10(6) on gel filtration and an amino acid content virtually identical with that of monomeric peptide alpha 1 CB6. The material could be adsorbed on affinity gels containing immobilized anti-(alpha 1 CB6-peptide non-helical region) antibodies and was an inhibitor of haemagglutination by the same antibodies of alpha 1 CB6-peptide-coated sheep erythrocytes. Periodate treatment of the material had no effect. Alkali hydrolysates were shown to contain two unknown amino acids, which were purified by gel filtration and ion-exchange chromatography in volatile buffers and are believed to be components of the mature cross-link of collagen.

Sign in / Sign up

Export Citation Format

Share Document