High activity of dipeptidyl peptidase I in Type 1 and 2A fibres of rat skeletal muscle
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Anatomy
Link
http://link.springer.com/content/pdf/10.1007/BF01675339.pdf
Reference8 articles.
1. BROOKE, M. H. & KAISER, K. K. (1970) Three ‘myosin adenosine triphosphatase systems. The nature of their pH lability and sulphydryl dependence.J. Histochem. Cytochem. 18, 670–2.
2. KAR, N. C. & PEARSON, C. M. (1978a) Dipeptidyl peptidases in human muscle disease.Clin. Chim. Acta 82, 185–192.
3. KAR, N. C. & PEARSON, C. M. (1978b). Muscular dystrophy and activation of proteinases.Muscle & Nerve 1, 308–13.
4. LOJDA, Z., GOSSRAU, R. & SCHIEBLER, T. H. (1979)Enzyme Histochemistry. A Laboratory Manual. Berlin, Heidelberg, New York: Springer-Verlag.
5. PARSONS, M. E. & PENNINGTON, R. J. T. (1976) Separation of rat muscle aminopeptidase.Biochem. J. 155, 375–81.
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1. Carboxylic ester hydrolases in mitochondria from rat skeletal muscle;The Histochemical Journal;1990-02
2. Dipeptidyl peptidases in the soleus muscle of the rat before and after treatment with 5-hydroxytryptamine;Histochemistry;1988
3. Localization of cathepsin B activity in fibroblasts and chondrocytes by continuous monitoring of the formation of a final fluorescent reaction product using 5-nitrosalicylaldehyde;The Histochemical Journal;1987-09
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