Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
Polish version English version Language
enabled [disable] Abstract
Number of results

Results found: 3

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
1

Function, properties and clinical significance of N-acetyl-beta-D- /HEX/

100%
Ostrowska L., Zwierz K., Koniusz Z., Gindzienski A.
Postępy Higieny i Medycyny Doświadczalnej
|
1993
|
vol. 47
|
issue 1
67-80
EN
Function, and consequence of the of (HEX A> or , were described. The diagnostic value of the HEX determination in the and was reviewed.
2
Content available remote

Effect of cadmium on collagen content and solubility in rat bone.

100%
Galicka A., Brzóska M. M., Średzińska K., Gindzienski A.
|
|
vol. 51
|
issue 3
825-829
EN
The toxic action of cadmium in the bone tissue is known, but its mechanisms are still unexplained. We examined whether Cd influences collagen content and its solubility in the femoral bone of three-week-old female rats exposed to 5 or 50 mg Cd/l in drinking water. Non-cross linked collagen was extracted with 0.5 M acetic acid, and two acid-insoluble collagen fractions were extracted with pepsin and 4.0 M guanidine hydrochloride, respectively. SDS/PAGE showed the presence of two collagen types, I and V, in all three extracted fractions. Exposure of rats to Cd for 6 months increased the amount of acid-soluble collagens type I and V and decreased the level of acid-insoluble collagens. The amount of total collagen extracted from the bones of rats exposed to 50 mg Cd/l was reduced by about 14% as compared to control and those intoxicated with 5 mg Cd/l. The solubility of type I bone collagen (determined as the percentage of acetic-soluble fraction of total collagen) was increased 2.9- and 3.0-fold in rats intoxicated with 5 and 50 mg Cd/l, respectively. Similarly, the solubility of type V collagen was increased 2.3- and 2.7-fold, respectively. Our results indicate that Cd treatment affects bone collagen by decreasing its content and increasing its solubility.
3
Content available remote

A novel Gly to Arg substitution at position 388 of the α1 chain of type I collagen in lethal form of osteogenesis imperfecta.

88%
Galicka A., Wolczynski S., Lesniewicz R., Chyczewski L., Gindzienski A.
|
2002
|
vol. 49
|
issue 2
443-450
EN
Cultured skin fibroblasts from a proband with a lethal form of osteogenesis imperfecta produce two forms of type I collagen chains, with normal and delayed electrophoretic migration; collagen of the proband's mother was normal. Peptide mapping experiments localized the structural defect in the proband to α1(I) CB8 peptide in which residues 123 to 402 are spaned. Direct sequencing of amplified cDNA covering this region revealed a G to A single base change in one allele of the α1(I) chain, that converted glycine 388 to arginine. Restriction enzyme digestion of the RT-PCR product was consistent with a heterozygous COL1A1 mutation. The novel mutation conforms to the linear gradient of clinical severity for the α1(I) chain and results in reduced thermal stability by 3°C and intracellular retention of abnormal molecules.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.