• 대한수의학회지
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• 제39권3호
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• pp.478-488
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• 1999

The contents of histidine dipeptides, a metabolic products of muscle protein, were investigated to compare muscle composition among the 9 domestic animals including cattle. In major domestic animals, analyzed the effects of age, part and sex of the animals on their muscle composition. Large amounts of carnosine($68.63{\pm}17.41{\mu}mol/g$) were detected in cattle and it was higher than other animals. Whereas the content of anserine showed high level in order of turkey, chickens and duck. The ratio of carnosine and anserine(C/A ratio) was different depending on the animal species. Statistical data indicated that difference among species was significant(p < 0.05). The contents of histidine dipeptides in heated muscle by boiling for 40 minutes at $110^{\circ}C$ was similar to thoes of raw muscle. C/A ratio in heated muscle was not different from that of raw muscle, indicating that no change has been made after heating process. The contents of carnosine and anserine were different according to the parts of their muscle. Especially chuck of the mammalian showed extremely low level of histidine dipeptides compared with other parts, while C/A ratio maintained certain level regardless of age, part, sex. Therefore, based on the content of histidine dipeptides, could be found the difference of muscle composition among the species. Also C/A ratio of horse, pig, cattle, duck, sheep and turkey were characteristic respectively.

• 식물조직배양학회지
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• 제21권4호
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• pp.201-206
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• 1994

Glycine, valine, alanine과 histidine의 수송은 모든 실험된 중성 아미노산에 의해 경쟁적인 방해를 당하였다.그리고 reciprocal 연구 결과로 이들 중성 아미노산들은 서로 carrier reciprocal의 활성부위를 점유하기위해 경쟁하므로 같은 운반자를 소유한다. Histidine은 전하를 띄우지 않은 상태로 중성 아미노산 운반자를 통해서 능동수송된다. 중성 운반자의 $K_m$ 값은 아미노산이 운반자에 대한 친화성에 따라서 3가지로 분류하였다. 0.1 mM 보다 작은 값, 0.1 mM에서 0.5 mM 사이에 있는 값고 0.5 mM 보다 큰 값이다. $V_{max}\;는\;3.12mol{\cdot}h^{-1}{\cdot}g{\;}fresh{\;}weight^{-1}\;과\;15.1\;{\mu}mole{\cdot}h^{-1}{\cdot}g{\;}fresh{\;}weight^{-1}$ 사이에 있다. 중성 아미노산은 아미노산 한개당 수소이온 한개가 동반수송되고, $K^{+}$ 한개가 전하보상을 위해서 배출된다. Histidine 분자도 1 분자당 1개의 수소이온과 동반수송되나 전하를 띄운 histidine 분자로부터 수소이온 한개가 배지로 떨어져 나오므로 동반수송된 수소이온의 움직임을 일시적으로 측정 할 수 없다.

• Journal of Microbiology
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• 제33권2호
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• pp.142-145
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• 1995

The pumb gene encoding a basic amino acid transport protein in Neurospora crassa could be cloned by using a mutant strain defective in pmb gene as a host strain, using a negative selection on the media containing amino acid analogue canavanine. To select positive transformants of the genes for cloning, an auxotrophic marker (his-2) was added to a pmb mutant strain by mating ; a triple mutant (pmn : pmb : his-2) was constructued by crossing a strain defective in basic amino acid transport system (# 1683-bat um 535 "A") to a double mutant strain defective in neutral amino acid transport and histidine production (mitrol : his-2 "a"). Crossing was performed on synthetic crossing (SC) media containing histidine. The pmn : pmb and pmn :pmb : his-2 strains were selected among the progeny colonies from crosses on plates containing 5- .mu.g/ml para-fluoro-phenylalanine (PFPA), 200 .mu.g/ml canavanine, and 500 .mu.g/ml histidine. The selected colonies were cultured on minimal media with or without histidine for discarding pmn : pmb strain, because the pmn : pmb : his -2 strain grows only on histidine containing media. The pmn :pmb : his-2 strain selected can be used as a host strain for the cloning of the pmb and the pmn genes from a Neurospora genomic library by means of positive selections.

• 대한임상검사과학회지
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• 제43권2호
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• pp.33-42
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• 2011

Zinc plays a key role in genetic expression, cell division, and cell growth and is essential for the functions of more than 450 metalloenzyme. There are high concentrations of zinc in pigment epithelium in bullfrog eye. Zinc deficiency causes night blindness and abnormal dark adaptation. The purpose of this study was to identify ERG (electroretinogram) b-wave sensitivity during light and dark adaptation in bullfrog retina after zinc and zinc chelators treatment such as histidine and TSQ (N-(6-methoxy-8-qunolyl)-p-toluenesulfon amide). Especially, we focused whether histidine act as a zinc chelator in the Muller cell. The results of our study are summarized as follows: 1) Both zinc and histidine elevated ERG b-wave amplitude and threshold in Muller cells by accelerating rhodopsin regeneration time and increased a-peak absorbance during light adaptation. 2) TSQ reduced those by prolonging rhodopsin regeneration time and decrement of a-peak absorbance during light adaptation. 3) Zinc shortened rhodopsin regeneration time and prolonged a-peak absorbance. These results suggested that histidine may act as a zinc-mediated transporter in presynaptic Muller cell membrane rather than zinc chelator and acts as a GABA-receptor inhibitor which blocks $Cl^-$ influx to the postsynapse.

• Journal of Microbiology and Biotechnology
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• 제9권1호
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• pp.62-69
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• 1999

In order to investigate the critical amino acid residues involved in the catalytic activities of $\beta$-cyclodextrin glucanotransferase ($\beta$-CGTase) excreted by Bacillus firmus var. alkalophilus, the amino acid residues in $\beta$-CGTase were modified by various site-specific amino acid modifying reagents. The cyclizing and amylolytic activities of $\beta$-CGTase were all seriously reduced after treatment with Woodward's reagent K (WRK) modifying aspartic/glutamic acid, N-bromosuccinimde (NBS) modifying tryptophan, and diethylpyrocarbonate (DEPC) modifying histidine residues. The roles of tryptophan and histidine residues in $\beta$-CGTase were further investigated by measuring the protection effect of various substrates during chemical modification, comparing protein mobility in native and affinity polyacrylamide gel electrophoresis containing soluble starch, and comparing the $K_m$ and $V_{max}$ values of native and modified enzymes. Tryptophan residues were identified as affecting substrate-binding ability rather than influencing catalytic activities. On the other hand, histidine residues influenced catalytic ability rather than substrate-binding ability, plus histidine modification had an effect on shifting the optimum pH and pH stability.

• 한국응용약물학회:학술대회논문집
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• 한국응용약물학회 1994년도 춘계학술대회 and 제3회 신약개발 연구발표회
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• pp.180-180
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• 1994

Farnesyl protein transferase는 Ras precursor의 C-terminal에 있는 cystein residue에 farnesyl group을 결합시키는 효소다. 이 효소를 bovine testis에서 30-50% ammonium sulfate fractionation, DEAE-sephacel ion exchange, Sephacryl s-300 gel filtration, hexapeptide(KKCVIM) affinity chromatography를 통해 30000배로 분리하였다. 분리된 효소는 gel filtration시 약 100kDa으로, SDS-polyacrylamide 전기영동시 50kDa의 인접한 두 bands로 나타났고 이것은 $\alpha$, $\beta$ subunits으로 생각되었다. $\alpha$ subunit을 encoding하는 RAM2 유전자를 site directed mutagenesis로 145번의 histidine을 aspartate로, 140번의 aspartate를 asparagine 으로 바꾸었더니 optimal pH와 $K_{m}$ 값이 변했다. Diethyl pyrocarbonate로 histidine residues를 chemical modification시켰을때 효소의 활성이 저하되었다. 145번 histidine이 aspartate로 바뀐 돌연변이효소에서 비교적 느리게 활성이 저하되므로 145번 histidine이 이 효소의 active site에 있을것으로 추측된다.

• Bulletin of the Korean Chemical Society
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• 제31권11호
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• pp.3217-3220
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• 2010

The electronic structures and bonding configuration of histidine on Ge(100) have been investigated with various sample treatments using core-level photoemission spectroscopy (CLPES). Interpretation of the Ge 3d, C 1s, N 1s, and O 1s core level spectra being included in these systems revealed that both the imino nitrogen in the imidazole ring and the carboxyl group in the glycine moiety concurrently participate in the adsorption of histidine on a Ge(100) surface at 380 K. Moreover, we could clearly confirm that the imino nitrogen with a free lone pair in the imidazole group adsorbs on Ge(100) more strongly than the carboxyl group in the glycine moiety by examining systems annealed at various temperatures.

• BMB Reports
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• 제40권1호
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• pp.125-129
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• 2007

Neurofilament-L (NF-L) is a major element of the neuronal cytoskeleton and is essential for neuronal survival. Moreover, abnormalities in NF-L result in neurodegenerative disorders. Carnosine and the related endogeneous histidine dipeptides prevent protein modifications such as oxidation and glycation. In the present study, we investigated whether histidine dipeptides, carnosine, homocarnosine, or anserine protect NF-L against oxidative modification during reaction between cytochrome c and $H_2O_2$. Carnosine, homocarnosine and anserine all prevented cytochrome c/$H_2O_2$-mediated NF-L aggregation. In addition, these compounds also effectively inhibited the formation of dityrosine, and this inhibition was found to be associated with the reduced formations of oxidatively modified proteins. Our results suggest that carnosine and histidine dipeptides have antioxidant effects on brain proteins under pathophysiological conditions leading to degenerative damage, such as, those caused by neurodegenerative disorders.

• 약학회지
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• 제54권5호
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• pp.334-340
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• 2010

We investigated whether poly-L-histidine (PLH) significantly affect mucin release from cultured airway epithelial cells. Confluent primary hamster tracheal surface epithelial (HTSE) cells were metabolically radiolabeled with $^$^3H$$glucosamine for 24 hr and chased for 30 min in the presence of PLH to assess the effect on $^3H$-mucin release. PLH 9,850 and PLH 6,700 specifically inhibit mucin release from airway goblet cells without significant cytotoxicity. This finding suggests that poly-L-histidine might function as an airway mucoregulative agent.

• Bulletin of the Korean Chemical Society
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• 제22권3호
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• pp.261-262
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• 2001