Structure and function ofl-glutamate decarboxylase

Jang-Yen Wu; Whei-Mei Huang; Lori Reed-Fourquet; Jun Bao; Britto nathan; Elliott Wu; Wuhong Tsai; Britto P. Nathan

doi:10.1007/BF00966085

Structure and function ofl-glutamate decarboxylase

Jang-Yen Wu
, Whei-Mei Huang
, Lori Reed-Fourquet
, Jun Bao
, Britto nathan
, Elliott Wu
, Wuhong Tsai
, Britto P. Nathan

Eastern Illinois University

University of Kansas
Baylor College of Medicine
Academia Sinica

Producción científica › revisión exhaustiva

Idioma original	American English
Publicación	Neurochemical Research
Volumen	16
DOI	https://doi.org/10.1007/BF00966085
Estado	Published - mar 1 1991

Disciplines

Biochemistry
Endocrinology
Biology
Internal Medicine

Acceder al documento

10.1007/BF00966085Licencia: Unspecified

Otros archivos y enlaces

https://link.springer.com/article/10.1007/BF00966085

Citar esto

@article{e6499b24ccdb43889412ae3693489cc4,

title = "Structure and function ofl-glutamate decarboxylase",

author = "Jang-Yen Wu and Whei-Mei Huang and Lori Reed-Fourquet and Jun Bao and Britto nathan and Elliott Wu and Wuhong Tsai and Nathan, \{Britto P.\}",

note = "Membrane boundl-glutamate decarboxylase (GAD) has been solubilized and partially purified from hog brain. The solubilized GAD appears to exist in two forms, α and β, differing in their size and electrophoretic mobility. The α form has similar mobility as that of the soluble GAD in 7.5\% and 5-25\% gradient polyacrylamide gel electrophoresis suggesting that they are similar in size and charge.",

year = "1991",

month = mar,

day = "1",

doi = "10.1007/BF00966085",

language = "American English",

volume = "16",

journal = "Neurochemical Research",

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TY - JOUR

T1 - Structure and function ofl-glutamate decarboxylase

AU - Wu, Jang-Yen

AU - Huang, Whei-Mei

AU - Reed-Fourquet, Lori

AU - Bao, Jun

AU - nathan, Britto

AU - Wu, Elliott

AU - Tsai, Wuhong

AU - Nathan, Britto P.

N1 - Membrane boundl-glutamate decarboxylase (GAD) has been solubilized and partially purified from hog brain. The solubilized GAD appears to exist in two forms, α and β, differing in their size and electrophoretic mobility. The α form has similar mobility as that of the soluble GAD in 7.5% and 5-25% gradient polyacrylamide gel electrophoresis suggesting that they are similar in size and charge.

PY - 1991/3/1

Y1 - 1991/3/1

UR - https://link.springer.com/article/10.1007/BF00966085

U2 - 10.1007/BF00966085

DO - 10.1007/BF00966085

M3 - Article

VL - 16

JO - Neurochemical Research

JF - Neurochemical Research

ER -