An improved method of plasma deproteination with sulphosalicylic acid for determining amino acids and related compounds

1972 ◽  
Vol 74 (2) ◽  
pp. 255-263 ◽  
Author(s):  
Angelo Mondino ◽  
Gianni Bongiovanni ◽  
Silvano Fumero ◽  
Lucia Rossi
2001 ◽  
Vol 183 (18) ◽  
pp. 5441-5444 ◽  
Author(s):  
Hikaru Suenaga ◽  
Mariko Mitsuoka ◽  
Yuko Ura ◽  
Takahito Watanabe ◽  
Kensuke Furukawa

ABSTRACT Biphenyl dioxygenase (Bph Dox) catalyzes the initial oxygenation of biphenyl and related compounds. Bph Dox is a multicomponent enzyme in which a large subunit (encoded by the bphA1 gene) is significantly responsible for substrate specificity. By using the process of DNA shuffling of bphA1 of Pseudomonas pseudoalcaligenes KF707 and Burkholderia cepaciaLB400, a number of evolved Bph Dox enzymes were created. Among them, anEscherichia coli clone expressing chimeric Bph Dox exhibited extremely enhanced benzene-, toluene-, and alkylbenzene-degrading abilities. In this evolved BphA1, four amino acids (H255Q, V258I, G268A, and F277Y) were changed from the KF707 enzyme to those of the LB400 enzyme. Subsequent site-directed mutagenesis allowed us to determine the amino acids responsible for the degradation of monocyclic aromatic hydrocarbons.


2018 ◽  
Vol 165 (12) ◽  
Author(s):  
Tomoko Koito ◽  
Syuku Saitou ◽  
Toshihiro Nagasaki ◽  
Syosei Yamagami ◽  
Toshiro Yamanaka ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document