Crystallization and Preliminary X-Ray Analysis of Thermoactinomyces vulgaris R-47 α-Amylase II
✍ Scribed by Shigehiro Kamitori; Tomoya Satou; Takashi Tonozuka; Yoshiyuki Sakano; Hiroshi Matsuzawa; Kenji Okuyama
- Book ID
- 115633739
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 357 KB
- Volume
- 114
- Category
- Article
- ISSN
- 1047-8477
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Enzymes that hydrolyze pullulan (1), such as pullulanases [1,2], isopullulanase [3], neopullulanases [4][5][6], and Thermoactinomyces vulgaris alpha-amylases [7,8] are useful in the production of various oligosaccharides from starch or pullulan . Recently, because of the commercial significance, man
## Abstract Nonglycosylated α‐amylase, a major component of human parotid saliva, has been crystallized by the vapor diffusion technique using 2‐methyl‐2,4‐pentanediol as the precipitant in the presence of CaCl~2~ at pH 9.0. The crystals are orthorhombic, space group __P__2~1~2~1~2~1~ with unit cel