## Abstract Circular dichroism spectra for acidβsoluble calfskin collagen, gelatin, and poly(proline) II in solution have been extended into the vacuum ultraviolet region. The extended spectrum of gelatin reveals that the circular dichroism of this unordered polymer is more closely related to the s
Collagenase induced changes in the circular dichroism spectrum of collagen
β Scribed by F. H. Chu; A. Lukton
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 356 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
The maximum at 220 nm in the circular dichroism spectrum of native collagen solution changed to a negative value after heat denaturation or collagenase hydrolysis. The enzyme induced rate of C1) change a t 220 nm was shown to be first order in collagen concentration. The specific rate constant k is actually a combined rate constant kfast and k,l,,v in which the ratio k,/k, is 4.1. The initial rates were linear with respect t o enzyme concentration, and the I<, was found to be 3.5 X 10-7 Ill. The rate of ultraviolet hyperchromicity at 220 nm on collagen hydrolysis was determined. The kf3't was the same as that obtained by C1).
Both methods may be readily wed to assay for collagenase activity.
The k,/k, ratio was 4.6.
π SIMILAR VOLUMES
Circular dichroism is an essential spectral property for probing chirality. 2] An interesting effect arises when an achiral guest chromophore is complexed in a chiral host. The guest becomes optically active, a phenomenon referred to as ΒͺinducedΒΊ circular dichroism (ICD). [3Β±5] The spectroscopic in
We compared changes in the fluorescence, circular dichroism (CD) and multiply charged electrospray ionization mass spectrometry (ESI-MS) spectra of three calcium (Ca 2 )-binding proteins upon the binding of Ca . The proteins used were rat brain calbindin D 28K and two deletion mutants, one lacking E