추천 제품
생물학적 소스
bovine liver
Quality Level
유형
Type III
양식
lyophilized powder
특이 활성도
≥20 units/mg protein
UniProt 수납 번호
저장 온도
−20°C
유전자 정보
cow ... GLUD1(281785)
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애플리케이션
L-Glutamic Dehydrogenase was used to catalyzes the conversion of isocitrate into a-ketoglutarate and carbon dioxide.
생화학적/생리학적 작용
Mammalian forms of this enzyme, including this bovine form, can use either NADP(H) or NAD(H) as coenzymes. L-glutamic dehydrogenase plays a unique role in mammalian metabolism. The reverse reaction catalyzed by this enzyme is the only pathway by which ammonia can become bound to the α-carbon atom of an α-carboxylic acid and thus, is the only source of de novo amino acid synthesis in mammalian species.
The bovine enzyme is characterized by three sets of properties:
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
The bovine enzyme is characterized by three sets of properties:
- It has a reversible concentration-dependent association, producing higher molecular weight forms.
- Forms tight enzyme-reduced coenzyme-substrate ternary complexes whose rates of dissociation modulate the steady-state reaction rates.
- Exhibits a wide variety of effects from the binding of any of a number of nucleotide modifiers.
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate.
포장
Package size based on protein content
단위 정의
One unit will reduce 1.0 μmole of α-ketoglutarate to L-glutamate per min at pH 7.3 at 25 °C, in the presence of ammonium ions.
물리적 형태
Contains citrate and potassium phoshate buffer salts.
분석 메모
Protein determined by biuret
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
개인 보호 장비
Eyeshields, Gloves, type N95 (US)
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