Changes in the Melting Characteristics of Bovine Tendon Collagen Induced by a Bacterial Collagenase
β Scribed by V.M. BERNAL; D.W. STANLEY
- Book ID
- 108811727
- Publisher
- Institute of Food Technologists
- Year
- 1986
- Tongue
- English
- Weight
- 278 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0022-1147
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π SIMILAR VOLUMES
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
## Abstract ## Background and Objective The treatment of calcaneal tendon injuries requires longβterm rehabilitation. Ultrasound (US) and lowβlevel laser therapy (LLLT) are the most used and studied physical agents in the treatment of tendon injuries; however, only a few studies examined the effec