• Proceedings of the Korean Society of Applied Pharmacology
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• 1993.04a
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• pp.166-166
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• 1993

만성 신부전환자에서 isoniazid(INH)의 약동학적 변화여부를 검토하고 특히 N-acetylation 대사능의 억제 여부를 평가함으로써 만성신부전환자에서 적정 INH 항결핵 요법율 위한 기본자료를 제공코자 하였다. 본 연구는 pararell group 디자인에 의한 일차 연구와 sequential 디자인에 의한 2차연구로 진행하였다. 일차 연구는 37명의 정상 성인군과 14명의 만성신부전 환자군을 대상으로 INH 400 mg 경구 투여 후 INH 및 AcINH의 약동학적 성상을 비교하였다. 이차연구는 만성신부전 환자에서 신이식에 따른 INH의 acetylation 대사능의 변화를 관찰코자 1차연구에 참여하고 성공적인 신이식을 받은 환자 10명을 대상으로 INH 및 AcINH의 약동학적 검토를 재시행하였으며, 이러한 연구 방법을 통하여 만성 신부전 환자에서 Acetylation 대사능의 변화를 검토하였다.

• Archives of Pharmacal Research
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• v.19 no.6
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• pp.502-506
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• 1996

Protein X is one of the subunits of pyruvate dehydrogenase complex. The biological role of this protein has not been fully elucidated, mainly because of the difficulty in its dissociation from the tightly bound dihydrolipoamide acetyltransferase-protein X subcomplex. We have found that the detachment of protein X from acetyltransferase subunit can be easily accomplished by the cycles of freezing and thawing proces. Several lines of evidence including sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequence analysis and acetylation with $[2^{14}C]$ pyruvate confirmed that the purified protein is protein X. The purified intact form of protein X was acetylated by $[2^{14}C]$ pyruvate in the presence of py-ruvate dehydrogenase subunit.The acetylation efficiency of this protein was lower than that of acetyltransferase and was not affected by the presence of acetyltransferase.

• Bulletin of the Korean Chemical Society
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• v.31 no.12
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• pp.3870-3871
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• 2010

• Korean Journal of Food Science and Technology
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• v.21 no.5
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• pp.714-720
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• 1989

Effects of acetylation on conformational changes of glycinin was studied using solvent perturbation, second derivative spectroscopy, near uv circular dichroism spectra and viscosity. Glycinin with purity of more than 93% was used for the experiment. Modification was carried out with acetic anhydride and glycinin with lysine residue modification of 0%, 28%, 65%, 85%, and 95% were used for the experiment. The result of solvent perturbation using some selected perturbants, such as glycerol, ethylene glycol, and dimethyl sulfoxide revealed that acetylation has caused increase In solvent accessibility of tyrosine residues from less than 40% in native protein to more than 70% for 95% acetylated glycinin. This was confirmed by second derivative spectroscopy. Near ultraviolet circular dichroism revealed that the spectra of native and acetylated glycinin were almost identical differing only in intensity and no other useful information could be derived from it. However, in the case of 95% acetylated glycinin the influence of tryptophan on the spectrum was more pronounced Specific viscosity of glycinin also increased by modification, the extent of which depended upon the degree of acetylation. These results supported that acetylation had caused globular conformation of glycinin to be expanded and denatured.

• Food Science of Animal Resources
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• v.41 no.4
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• pp.650-663
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• 2021

The objective of this study was to examine the relationship between meat quality attributes and the changes of sarcoplasmic protein acetylation and myofibrillar protein acetylation in lamb longissimus thoracis et lumborum muscles at different postmortem phases. Protein acetylation, color, pH, shear force, myofibril fragmentation index and cooking loss were measured. The total level of acetylated sarcoplasmic proteins showed a negative relation with pH, a positive relation with a^*, b^* and cooking loss at the pre-rigor phase. Sarcoplasmic proteins acetylation affected postmortem pH by regulating glycolysis, which in turn affects color and cooking loss. The total level of acetylated myofibrillar proteins showed a positive relation with shear force at the pre-rigor phase. Myofibrillar proteins acetylation affected meat tenderness by regulating muscle contraction. This study indicated that acetylation played a regulatory role of meat color, water-holding capacity, and tenderization process at early postmortem.

• Bulletin of the Korean Chemical Society
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• v.24 no.4
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• pp.519-520
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• 2003

• Bulletin of the Korean Chemical Society
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• v.25 no.2
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• pp.325-327
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• 2004

• Bulletin of the Korean Chemical Society
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• v.24 no.11
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• pp.1683-1685
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• 2003

• Journal of Microbiology and Biotechnology
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• v.18 no.9
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• pp.1529-1536
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• 2008

Acetylation of lysine residues in proteins is a reversible and highly regulated posttranslational modification. However, it has not been systematically studied in prokaryotes. By affinity immunoseparation using an anti-acetyllysine antibody together with nano-HPLC/MS/MS, we identified 125 lysine-acetylated sites in 85 proteins among proteins derived from Escherichia coli. The lysine-acetylated proteins identified are involved in diverse cellular functions including protein synthesis, carbohydrate metabolism, the TCA cycle, nucleotide and amino acid metabolism, chaperones, and transcription. Interestingly, we found a higher level of acetylation during the stationary phase than in the exponential phase; proteins acetylated during the stationary phase were immediately deacetylated when the cells were transferred to fresh LB culture medium. These results demonstrate that lysine acetylation is abundant in E. coli and might be involved in modifying or regulating the activities of various enzymes involved in critical metabolic processes and the synthesis of building blocks in response to environmental changes.

• Korean Journal of Food Science and Technology
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• v.20 no.5
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• pp.625-630
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• 1988

Phosphorylation of soy protein by sodium trimetaphosphate and acetylation of soy protein by acetic anhydride were performed. Then, the functional properties of modified soy proteins were compared with that of unmodified soy protein. Isolated soy protein prepared from defatted soybean flake had protein content of 92.7% as moisture-free basis. The phosphorylated soy protein showed higher solubility, foaming properties, and water holding capacity than unmodified soy protein. Acetylation of soy protein increased emulsification activity and foaming properties greatly, whereas decreased the solubility at pH 8.0. Isoelectric pHs of phosphorylated and acetylated soy protein were shifted to acidic regions(pH 3.0 and pH 4.0) from pH 5.0, which was the isoelectric pH of unmodified soy protein. Soy protein seems to be aggregated during phosphorylation and acetylation procedure, judging form Sepharose CL-4B gel filtration profiles. The modified soy proteins showed increased mobilities to anode direction in disc-gel electrophoresis.