A calcium-activated neutral proteinase (CANP)-specific endogenous inhibitor (calpastatin) was purified from bovine brain b y successive column chromatography. The purified inhibitor exhibited a major band on sodium dodecylsulfate polyacrylamide gel electrophoresis with an approximate molecular weigh
β¦ LIBER β¦
Purification of calcium-activated neutral proteinase (CANP) from purified myelin of bovine brain white matter
β Scribed by Arun K. Chakrabarti; Naren L. Banik
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 1019 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0364-3190
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## Abstract Of the Na, KβATPase activity in brain homogenates from 20β, 60β, and 120βdayβold rats, 1.4 to 2.6% was recovered in myelin. The relative specific activities, at 0.2 to 0.3 times the specific activities in the rat brain homogenates, did not decrease during development, and myelin from bo