• Applied Biological Chemistry
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• 제17권3호
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• pp.184-192
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• 1974

2N 염산의 존재하에 N-bromosuccinimide는 8-aminoquinoline과 수용액 중에서 반응하여 5,7-dibromo-8-aminoquinoline를 생성한다. 이 반응은 실온에서 용이하게 또 정량적으로 진행 한다. 본 연구에서 이 반응기구가 검토되었으며 N-bromosuccinimide를 사용하여 8-aminoquinoline의 미량정량을 위한 새로운 적정법이 확립되었다. 본 분석방법은 간단하고 신속하며 주어진 정량 범위내에서 비교적 높은 정확성을 나타내며, 실험오차는 ${\pm}1.78$%를 넘지않는다. 본 방법과 Bromimetry에 의한 8-aminoquinoline의 비교분석 결과도 보고한다.

• BMB Reports
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• 제31권2호
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• pp.139-143
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• 1998

The catabolic ${\alpha}-acetolactate$ synthase purified from Serratia marcescens ATCC 25419 was rapidly inactivated by the tryptophane-specific reagent, N -bromosuccinimide, and the arginine-specific reagent, phenylglyoxal. The enzyme was inactivated slowly by the cysteine-specific reagent N-ethylmaleimide. The second-order rate constants for the inactivation by N-bromosuccinimide, phenylglyoxal. and N -ethylmaleimide were $114,749M^{-1}min^{-1}$, $304.3M^{-1}min^{-1}$, and $5.1M^{-1}min^{-1}$, respectively. The reaction order with respect to N-bromosuccinimide, phenylglyoxal, and N-ethylmaleimide were 1.5,0.71, and 0.86, respectively. The inactivation of the catabolic aacetolactate synthase by these modifying reagents was protected by pyruvate. These results suggest that essential tryptophane, arginine, and cysteine residues are located at or near the active site of the catabolic ${\alpha}-acetolactate$ synthase.

• 대한화학회지
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• 제31권5호
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• pp.476-478
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• 1987

• Archives of Pharmacal Research
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• 제13권4호
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• pp.367-370
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• 1990

A novel method for the microdetermination of vitamin A in its pure state and pharmaceutical preparation using NBS is reported. The new method is easy, simple and accurate.

• 대한화학회지
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• 제46권4호
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• pp.402-404
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• 2002

• 한국미생물·생명공학회지
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• 제34권2호
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• pp.121-128
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• 2006

Bacillus alcalophilus AX2000으로부터 xylanase를 정제한 후 효소의 활성부위를 조사하기 위하여 여러 가지 화학수식제를 사용하여 효소활성의 저해도를 측정하였다. 여러 가지 화학 수식제 중에서 carbodiimide와 N-bromosuccinimide가 효소 활성을 완전히 저해시켜 glutamic acid또는 aspartic acid 잔기와 tryptophan 잔기가 효소의 활성부위에 관여하리라 추측되었다. 각각의 경우에 효소 실활은 수식제의 첨가농도에 따라 pseudo first-order kinetics 양식을 보여주었으며, carbodiimide와 N-bromosuccinimide는 각각 비경쟁적 저해와 경쟁적 저해방식을 나타내었다. 기질첨가에 의한 효소활성 보호실험을 통하여 tryptophan 잔기가 기질결합부위라 판단 되었다. 효소 실활속도의 분석에 의해 효소활성에는 2개의 glutamic acid 또는 aspartic acid 잔기와 1개의 tryptophan 잔기가 관여하는 것으로 나타났다.

• 생명과학회지
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• 제15권4호
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• pp.633-640
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• 2005

Bacillus pumilus TX703으로부터 xylanase를 정제한 후 효소의 활성부위를 조사하기 위하여 여러 가지 화학수식제를 사용하여 효소활성의 저해도를 측정하였다. 여러 가지 화학수식제 중에서 carbodiimide와 N-bromosuccinimide가 효소활성을 완전히 저 해시 켜 glutamic acid 또는 aspartic acid 잔기와 tryptophan 잔기가 효소의 활성부위에 관여하리라 추측되었다. 각각의 경우에 효소 실활은 수식제의 첨가농도에 따라 pseudo first-order kinetics 양식을 보여주었으며, car-bodiimide와 N-bromosuccinimide는 각각 비경쟁적 저해와 경쟁적 저해방식을 나타내었다. 기질첨가에 의한 효소활성 보호실험을 통하여 tryptophan 잔기가 기질결합부위라 판단되었다. 효소실활속도의 분석에 의해 효소활성에는 2개의 glutamic acid 또는 aspartic acid 잔기와 1개의 tryptophan 잔기가 관여하는 것으로 나타났다.

• BMB Reports
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• 제32권3호
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• pp.294-298
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• 1999

Myo-inositol monophosphate phosphatase is a key enzyme in the phosphoinositide cell-signaling system. Incubation of myo-inositol monophosphate phosphatase from porcine brain with N-bromosuccinimide (NBS) resulted in a time-dependent loss of enzyme activity. The inactivation followed pseudo-first-order kinetics with the second-order rate constant of $3.8{\times}10^3\;M^{-1}min^{-1}$. The time course of the reaction was significantly affected by the substrate myo-inositol-1-phosphate, which afforded complete protection against the loss of catalytic activity. Spectrophotometric studies indicated that about one oxindole group per molecule of enzyme was formed following complete loss of enzymatic activity. It is suggested that the catalytic function of myo-inositol monophosphate phosphatase is modulated by the binding of NBS to a specific tryptophan residue at or near the substrate binding site of the enzyme.

• BMB Reports
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• 제31권3호
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• pp.258-263
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• 1998

Acetolactate synthase (ALS) is the common enzyme in the biosynthetic pathways leading to leucine, valine, and isoleucine. Tobacco ALS was expressed in E. coli and purified to homogeneity. The recombinant tobacco ALS was inactivated by thiol-specific reagents, N-ethylmaleimide (NEM) and 5,5'-dithio-bis-(2-nitrobenzoic acid) (DTNB). Inactivation of the ALS by NEM followed pseudo-first order kinetics and was first order with respect to the modifier. The substrate pyruvate protected the enzyme against the inactivation by NEM and DTNB. Extrapolation to complete inactivation of the enzyme by DTNB showed modification of approximately 2 out of 4 total cysteinyl residues (or 2 cysteinyl and 1 cysteinyl residues), with approximately 1 residue protected by pyruvate. The tobacco ALS was also inactivated by the tryptophanspecific reagent, N-bromosuccinimide (NBS), and was similarly protected by pyruvate. The kinetics of the inactivation was first-order with respect to NBS. The present data suggest that cysteinyl and tryptophanyl residues play a key role in the catalytic function of the enzyme.

• Archives of Pharmacal Research
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• 제16권2호
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• pp.152-154
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• 1993

By using N-bromophthalimide (NBP) as halonium ion source for the Hofmann rearrangement, a series of primary amide could be ocnverted to the corresponding cabamate in excellent yields. So NBP was throught to be very effective and practical halonium ion source for the Hofmann rearrangement.