scholarly journals Desmosine and isodesmosine contents and elastase activity in normal and cirrhotic rat liver

1983 ◽  
Vol 214 (3) ◽  
pp. 1023-1025 ◽  
Author(s):  
V Velebný ◽  
E Kasafírek ◽  
J Kanta

The contents of desmosine and isodesmosine, the cross-linking amino acids of elastin, were increased 4-fold in rat liver with carbon tetrachloride-induced cirrhosis, which suggests that insoluble elastin accumulates in cirrhosis. Elastase activity in the cirrhotic liver, as determined with 3-carboxypropionyl-L-alanyl-L-alanyl-L-alanine p-nitroanilide, was 17% less than in the normal liver; no change was found when Congo Red-elastin was used as a substrate.

2014 ◽  
Vol 900 ◽  
pp. 3-6 ◽  
Author(s):  
Jing Wang ◽  
Wei Fang ◽  
Yuan Yuan ◽  
Xiao Ming Liu

In order to improve thermal stability of Poly (Vinyl Chloride), a kind of thermal reversible cross-linking agents, the end cyclopentadienyl ethanethiol salts, sodium cyclopentadienyl ethyl mercaptan (CPD-C2H4SNa) was synthesized in this paper. The DSC results proved that the prepared CPD-C2H4SNa has obvious thermal reversible characteristics and the thermal reversible temperature was at 177 °C. The effects of cross-linking agent amount, cross-linking reactive time and temperature on flexible PVC compounds were evaluated through gel content testing. It was showed that the cross-linking agent with 3 Phr is optimum for PVC compounds. Moreover, both the cross-linking reactive time and temperature has effects on gel content of PVC compounds. The gel content of CPD-C2H4SNa cross-linked PVC compounds reaches maximum at 76% for 20 min at 160 °C.The static thermal stability of flexible PVC was measured according to congo red method. The results showed that the thermal stability of PVC compounds was enhanced with increasing cross-linking agent amount.


1972 ◽  
Vol 127 (1) ◽  
pp. 261-269 ◽  
Author(s):  
R. John ◽  
J. Thomas

1. Elastins were isolated from the visceral pleuras and parenchymas of lungs of humans of different ages. 2. The elastin content of pleuras increased whereas that of parenchymas remained constant with increasing age. 3. The amino acid compositions and carbohydrate contents of elastins isolated from both pulmonary tissues changed in the same way with increasing age of the subjects. These changes were similar to those observed in elastins isolated from the aorta. 4. Similar glycoproteins were isolated from pleuras and aortas, and were more difficult to extract from the elastins of older subjects. Contamination with these glycoproteins was responsible for the changes in composition of elastin, as the age of the tissue from which it was extracted increased. 5. The amount of the cross-linking amino acids desmosine and isodesmosine was lower in elastins isolated from both aorta and pulmonary tissues of senile subjects than those from younger subjects.


1988 ◽  
Vol 74 (5) ◽  
pp. 485-489 ◽  
Author(s):  
Taisuke Morimoto ◽  
Akira Tanaka ◽  
Yoshiro Taki ◽  
Masashi Noguchi ◽  
Naoki Yokoo ◽  
...  

1. Changes in the concentrations of respiratory components, phosphorylative activity, the cytochrome oxidase activity of mitochondria and the hepatic adenylate energy charge level (in situ) were studied in cirrhotic rat liver induced by carbon tetrachloride (CCl4). 2. In the cirrhotic liver mitochondria, concentrations of cytochrome a(+ a3), cytochrome b, coenzyme Q9 and coenzyme Q10 increased significantly to 2.44 ± 0.02 × 10−10 (mean ± se), 1.37 ± 0.05 × 10−10, 25.57 ± 0.47 × 10−10 and 5.39 ± 0.26 × 10−10 mol/mg of mitochondrial protein, respectively, compared with 1.83 ± 0.03 × 10−10, 1.22 ± 0.02 × 10−10, 16.24 ± 0.39 × 10−10 and 1·81 ± 0.07 × 10−10 in normal rats [P < 0.001 for cytochrome a(+ a3), coenzyme Q9 and coenzyme Q10, and P < 0.01 for cytochrome b]. 3. Concentrations of flavoprotein and pyridine nucleotides decreased significantly to 13.33 ± 0.14 × 10−10 and 45.68 ± 1.59 × 10−10 mol/mg of mitochondrial protein, respectively, compared with 14.79 ± 0.33 × 10−10 and 86.26 ± 1.83 × 10−10 in normal rats (P < 0.001). There was no significant difference in the concentration of cytochrome c(+ c1). 4. Cytochrome oxidase activity per unit of cytochrome a(+ a3) increased significantly to 67.43 ± 1.71 atoms O s−1 mol−1, compared with 55.77 ± 1.16 in normal rats (P < 0.001). By contrast, phosphorylative activity per unit of cytochrome a(+ a3) decreased significantly in the cirrhotic liver to 10.40 ± 0.36 s−1 compared with 13.43 ± 0.49 in normal rats (P < 0.001). The total adenine nucleotide concentration and the hepatic energy charge level decreased significantly in the cirrhotic liver to 3.420 ± 0.075 μmol/g of wet liver and 0.806 ± 0.003, respectively, compared with 3·854 ± 0.088 and 0.841 ± 0.004 in normal rats (P < 0.001). 5. It is concluded that in mitochondria obtained from CCl4-induced cirrhotic rat liver in which the energy charge level is decreased, cytochrome oxidase activity per unit of cytochrome a(+ a3) is increased in association with an increase in cytochrome a(+ a3) concentration.


2021 ◽  
Vol 23 (6) ◽  
pp. 3761-3770
Author(s):  
Jianfeng Zhao ◽  
Ruixue Zhu ◽  
Xiting Zhang ◽  
Bowu Zhang ◽  
Yancheng Liu ◽  
...  

Mechanisms of UV light-enabled strong oxidizing capacity of tetrazolium salts and their oxidization towards proteins were first elucidated.


Author(s):  
Stephen Keller ◽  
Anjan K. Ghosh ◽  
Ajit K. Ghosh ◽  
Gerard M. Turino ◽  
Ines Mandl

1993 ◽  
Vol 4 (2) ◽  
pp. 223-232 ◽  
Author(s):  
J A McNew ◽  
K Sykes ◽  
J M Goodman

A peptide corresponding to an efficient peroxisomal targeting sequence, the carboxy terminal 12 amino acids of PMP20 from Candida boidinii, was employed as an affinity ligand to search for a peroxisomal targeting receptor. Two proteins from yeast extracts with apparent molecular masses of 20 and 80 kDa were detected by chemical cross-linking to radioiodinated peptide. Both proteins were present in cytosolic supernatants. The 20-kDa species did not cross-link to a control peptide with reversed sequence, whereas the 80-kDa protein cross-linked to both peptides. The cross-linking assay was used to purify the 20-kDa protein from Saccharomyces cerevisiae. Partial protein sequencing identified this protein as cyclophilin, the product of the CYP1 gene. This protein, a peptidyl-prolyl cis-trans isomerase, is the yeast homologue of the protein that mediates the immunosuppressant effects of the drug cyclosporin A (CsA). Cross-linking of peptide to cyclophilin was inhibited by CsA. The cross-linking of cyclophilin to the PMP20-derived peptide was unanticipated because the peptide contains no prolines. The CYP1-encoded protein was not required to target proteins to peroxisomes because this organelle appeared to be assembled normally in a CYP1-disrupted strain. Furthermore, the final three amino acids of the peptide, which are critical for peroxisomal sorting, were not required for cross-linking to cyclophilin. We conclude that either cyclophilin is playing a nonessential facilitating role in peroxisomal targeting or that the interaction of the targeting peptide to cyclophilin is mimicking an interaction with an unidentified substrate or effector of cyclophilin.


2006 ◽  
Vol 110 (11) ◽  
pp. 5315-5320 ◽  
Author(s):  
B. Husár ◽  
S. Commereuc ◽  
I. Lukáč ◽  
Š. Chmela ◽  
J. M. Nedelec ◽  
...  

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