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Partial Purification and Characterization of Glutaminase fromLactobacillus reuteriKCTC3594

✍ Scribed by Jeong-Min Jeon; Hae-In Lee; Sang-Hyun Han; Chung-Soon Chang; Jae-Seong So

Book ID
107565407
Publisher
Springer-Verlag
Year
2009
Tongue
English
Weight
189 KB
Volume
162
Category
Article
ISSN
0273-2289

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Purification and characterization of aci
Purification and characterization of acid urease fromLactobacillus fermentum
✍ Shigeya Kakimoto; Yasuhiro Sumino; Kenji Kawahara; Eiichirou Yamazaki; Isamu Nak πŸ“‚ Article πŸ“… 1990 πŸ› Springer 🌐 English βš– 609 KB

Acid urease was purified to an electrophoretically homogeneous state, and the molecular weight was estimated to be 220 000. The enzyme consisted of three kinds of subunits, designated a, fl and 7z, with molecular weights of 67000, 16800 and 8600, respectively, in a (al f127q)2 structure. The isoelec