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11. |
Keratoconus corneas: Increased gelatinolytic activity appears after modification of inhibitors |
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Current Eye Research,
Volume 12,
Issue 6,
1993,
Page 571-581
BrownD.,
ChwaM. M.,
OpbroekA.,
KenneyM. C.,
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摘要:
We examined the metalloproteinase activity from normal and keratoconus corneal extracts. No differences were detected in the total amount of the metalloproteinase or its physical form of activation. However, there was a significant elevation in enzymatic activity in the keratoconus extracts after chemical modification of inhibitory elements. This suggests either a difference in the enzymatic capabilities of keratoconus corneas or, as suggested previously, a decrease in the amount of TIMP (tissue inhibitor of metalloproteinase) present in the tissue.
ISSN:0271-3683
DOI:10.3109/02713689309001835
出版商:Taylor&Francis
年代:1993
数据来源: Taylor
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12. |
Evidence that the chick lens cytoskeletal protein CP 49 belongs to the family of intermediate filament proteins |
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Current Eye Research,
Volume 12,
Issue 6,
1993,
Page 583-588
OriiHidefumi,
AgataKiyokazu,
SawadaKaichiro,
EguchiGoro,
MaiselHarry,
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摘要:
A partial cDNA sequence for chick lens beaded-filament protein CP 49 showed the greatest similarity to the sequence of acidic cytokeratins, especially human cytokeratin 18. The predicted amino acid sequence of chick CP 49 corresponded to the entire coil 1a region of the rod domain of human cytokeratin 18, spacer 1, coil 1b, spacer 2 and about half of coil 2. For this sequence of 242 amino acids, there was an overall 38% identity and 76.8% similarity between the chick CP 49 and human cytokeratin 18. This is further evidence that CP 49 belongs to the family of intermediate filament proteins.
ISSN:0271-3683
DOI:10.3109/02713689309001836
出版商:Taylor&Francis
年代:1993
数据来源: Taylor
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