A new proteolytic measurement of serum mitochondrial aspartate aminotransferase was evaluated using cytosolic aspartate aminotransferase inactivating protease. Some of the proteases, such as, c(-chymotrypsin, subtilisin and cytosolic aspartate aminotransferase inactivating protease 401 from Streptom
Serum mitochondrial aspartate aminotransferase in patients with polymyositis
โ Scribed by Saburo Ogasahara; Mitsuo Takahashi; Jin Kang; Shiro Yorifuji; Keiji Wada; Takanori Hazama; Hiroaki Takeuchi; Seiichiro Tarui
- Publisher
- John Wiley and Sons
- Year
- 1983
- Tongue
- English
- Weight
- 361 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0364-5134
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๐ SIMILAR VOLUMES
We studied a new proteinase K assay method for human serum mitochondrial aspartate aminotransferase. We found that proteinase K showed no inactivation of human mitochondrial aspartate aminotransferase isoenzyme and complete inactivation of cytosolic aspartate aminotransferase. Previous studies have
The optimal conditions for selective proteolytic inactivation of cytosolic aspartate aminotransferase (c-AST) to determine mitochondrial aspartate aminotransferase (m-AST) in serum were studied. Protease 401 was found to be effective over a pH range of 6.0-10.0. A pH of 9.5 with 0.5% albumin in the
p < 0.001 vs. Group I. ' Not statistically significant vs. controls p < 0.001 vs. Croups I + 11.
## Abstract Circadian variations in myoglobin levels were determined in 18 normal volunteers and in 10 patients with active polymyositis. In all the controls and in 9 of the 10 patients, serum myoglobin concentrations were highest at 9 AM, fell significantly during the day to reach a nadir between