• 제목/요약/키워드: arginine

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Pinus radiata 소나무의 정아내(頂芽內) Arginine함량(含量)의 시기적변화(時期的變化) (Seasonal Variation of Arginine in Buds of Pinus radiata in Relation to Flower Initiation)

  • 홍성옥;지 비 수이트
    • 한국산림과학회지
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    • 제33권1호
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    • pp.59-67
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    • 1977
  • 본(本) 실험(實驗)에서는 Pinus radiata의 정아내(頂芽內) 유리(遊離) arginine함량(含量)의 시기적(時期的) 변화(變化를) 화아분화(花芽分化)와 관련(關聯)하여 1974년(年) 5월(月)부터 1975년(年) 6월(月)까지의 기간(其間)에 걸쳐 연구(硏究)하였다. 사용(使用)된 정아(頂芽)는 뉴질랜드 로토루아시(市) 소재(所在) 임업연구소(林業硏究所) 포장(圃場)에 생장(生長)하고 있는 4개(個)의 Clone에서 채취(採取)하였으며, 전년도(前年度)에 개화(開花)하였던 가지의 정아(頂芽)를 arginine 분석(分析)에 이용(利用)하였다. 본(本) 연구(硏究)의 주요(主要)한 결과(結果)는 다음과 같다. 1. 일반적(一般的) 정아내(頂芽內) arginine의 함량(含量)은 4개(個) Clone에서 공(共)히 화아분화기(花芽分化期)인 12월(月)~3월(月)(북반구(北半球)의 6월(月)~9월(月)에 해당(該當)에 절정(絶頂)에 달(達)하였고 개화기(開花期)인 8월(月)~9월(月)에 가장 저조(低調)하였다. 2. 화아분화기중(花芽分化期中) arginine이 절정(絶頂)에 달(達)하는 회수(回數)는 각(各) Clone의 자화분화(雌花分化)의 주기수(週期數)(P. radiata에서는 1~3주기(週期)임) 대체(大體)로 일치(一致)하였다. 3. 개화량(開花量)이 많은 Clone은 적은 Clone에 비(比)하여 높은 arginine함량(含量)을 나타내었고 이러한 현상(現象)은 특(特)히 화아분화기(花芽分化期)에 더욱 현저(顯著)하였다. 4. 그러므로 정아내(頂芽內) Arginine의 함량(含量)은 화아분화(花芽分化)와 밀접(密接)한 관계(關係)가 있다고 사료(思料)된다.

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소시지 제조시 인산염 대체 소재로 L-Arginine의 활용 (Application of L-Arginine as a Substitute for Inorganic Polyphosphate in Pork Sausage Production)

  • 김용덕;이준수;박준현;박동철;전영승;인만진;오남순
    • Journal of Applied Biological Chemistry
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    • 제57권2호
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    • pp.171-174
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    • 2014
  • $\small{L}$-아르기닌의 알칼리성과 보습성을 식품에 활용하는 연구의 일환으로 폴리인산염 대신에 $\small{L}$-아르기닌을 0.25, 0.5, 1.0% (w/w) 첨가하여 소시지를 제조하고, 각각의 pH, 보수력, 유화 안정성 및 조직감을 조사하였다. 소시지의 pH는 $\small{L}$-아르기닌의 첨가량에 비례하여 증가하였으며, 수분함량은 $\small{L}$-아르기닌을 0.25% 이상, 유화 안정성은 0.5% 이상, 경도와 전단력은 1.0%를 첨가한 결과가 폴리인산나트륨을 0.5% 첨가한 소시지의 특성과 유사하였다. 인산염 0.5%와 $\small{L}$-아르기닌 0.5% 첨가 소시지에 대하여 관능 평가를 실시하였다. 조직감은 인산염을 사용한 시료가 $\small{L}$-아르기닌을 첨가한 시료보다, 맛과 전체적인 기호도에서도 $\small{L}$-아르기닌을 첨가한 소시지가 다소 우수한 것으로 평가되었다. 이상의 결과로부터 소시지 제조시 $\small{L}$-아르기닌은 인산염 대체 소재로 활용될 수 있으며 첨가량은 0.5%가 적절함을 확인할 수 있었다.

Chemical Modification of Brain Glutamate Dehydrogenase Isoproteins with Phenylglyoxal

  • Ahn, Jee-Yin;Cho, Eun-Hee;Lee, Kil-Soo;Choi, Soo-Young;Cho, Sung-Woo
    • BMB Reports
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    • 제32권5호
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    • pp.515-520
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    • 1999
  • Incubation of two types of glutamate dehydrogenase isoproteins from bovine brain with the arginine-specific dicarbonyl reagent phenylglyoxal resulted in a biphasic loss of enzyme activity. Reaction of the glutamate dehydrogenase isoproteins with phenylglyoxal caused a rapid loss of 53~62% of the enzyme activities and modification of two residues of arginine per enzyme subunit. Prolonged incubation of the glutamate dehydrogenase isoproteins with phenylglyoxal resulted in the modification of an additional four residues of arginine per enzyme subunit without further loss of the residual activities. Partial protection against inactivation was provided by the coenzyme NADH or substrate 2-oxoglutarate. The most marked decrease in the rate of inactivation was observed by the combined addition of NADH and 2-oxoglutarate, suggesting that the first two modified arginine residues are in the vicinity of the catalytic site. However, inactivation of the glutamate dehydrogenase isoproteins by phenylglyoxal appears to be partial with approximately 40% activity remained after an extended reaction time with excess reagent, suggesting that the modified arginine residues may not be directly involved in catalysis. The lack of complete protection by substrates also suggest the possibility that the modified arginine residues are not directly involved at the active site, and the partial loss of activity by the modification of arginine residues may be due to a conformational change. There were no significant differences between the two glutamate dehydrogenase isoproteins in sensitivities to inactivation by phenylglyoxal, indicating that the microenvironmental structures of the glutamate dehydrogenase isoproteins are very similar to each other.

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Positive Charge of Arginine Residues on Histone H4 Tail Is Required for Maintenance of Mating Type in Saccharomyces cerevisiae

  • Yeom, Soojin;Oh, Junsoo;Lee, Eun-Jin;Lee, Jung-Shin
    • Journal of Microbiology and Biotechnology
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    • 제28권9호
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    • pp.1573-1579
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    • 2018
  • Transcriptional gene silencing is regulated by the chromatin structure, which is by various factors including histones. Saccharomyces cerevisiae contains transcriptionally silenced regions such as telomeric regions and hidden mating (HM) loci. The positively-charged amino acids on the histone H4 tail were reported to be critical for the telomeric silencing in yeast, by interacting with Dot1, a specific methyltransferase for the $79^{th}$ lysine on histone H3. However, Dot1 did not affect gene silencing within HM loci, but whether the positively-charged amino acids on the H4 tail affect HM silencing has not been defined. To elucidate the function of the H4 tail on HM silencing, we created several MATa-type yeast strains bearing the substitution of arginine with alanine or lysine on the histone H4 tail and checked the sensitivity of MATa-type yeast to alpha pheromone. The arginine point mutants substituted by alanine (R17A, R19A, and R23A) did not show sensitivity to alpha pheromone, but only two arginine mutants substituted by lysine (R17K and R19K) restored the sensitivity to alpha pheromone-like wild type. These data suggested that the basic property of arginine at $17^{th}$ and $19^{th}$ positions in the histone H4 tail is critical for maintaining HM silencing, but that of the $23^{rd}$ arginine is not. Our data implicated that the positive charge of two arginine residues on the histone H4 tail is required for HM silencing in a manner independent of Dot1.

L-Arginine Ameliorates Kidney Function and Urinary Bladder Sensitivity in Experimentally-induced Renal Dysfunction in Rats

  • Mansour, Mahmoud A.;Al-Shabanah, Othman A.;El-Khashef, Hassan A.
    • BMB Reports
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    • 제36권4호
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    • pp.373-378
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    • 2003
  • Effects of L-arginine and NG-nitro-L-arginine methyl ester (L-NAME) on the renal dysfunction that is induced by cisplatin (CDDP) were investigated. A single dose of CDDP (7.5 mg/kg i.p.) induced renotoxicity, which was manifested by increasing the sensitivity of isolated urinary bladder rings to acetylcholine (ACh), together with a significant elevation of serum urea and creatinine, and a severe decrease in serum albumin. Moreover, renal dysfunction was further confirmed by a significant decrease of enzyme activities, such as glutathione peroxidase, GSH-Px (E.C 1.11.1.9), catalase (E.C 1.11.1.6), as well as a significant increase in lipid peroxides that were measured as malondialdhyde (MDA) in kidney tissue homogenates. The administration of L-arginine (70 mg/kg/d p.o in drinking water 5 d before and 5 d after the CDDP injection) significantly ameliorated the renotoxic effects of CDDP, as judged by restoring the normal responses of isolated bladder rings to Ach, and also by an improvement in a range of renal function indices, which included serum urea and creatinine concentrations and kidney weight. In addition, L-arginine prevents the rise of MDA, as well as a reduction of GSH-Px and catalase activities in kidney tissues homogenates. On the other hand, the administration of L-NAME (4 mg/kg/d p.o) resulted in no protection against renal dysfunction that was induced by CDDP treatment. The findings of this study suggest that L-arginine can attenuate kidney injury that is produced by CDDP treatment. In addition, L-arginine may be a beneficial remedy for CDDP-induced renal toxicity, and could be used to improve the therapeutic index of CDDP.

손바닥 선인장의 성분 특성 (Compositions of Opuntia ficus-indica)

  • 이영철;황금희;한동휴;김성대
    • 한국식품과학회지
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    • 제29권5호
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    • pp.847-853
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    • 1997
  • 손바닥 선인장(Opuntia ficus-indica var. saboten)의 성분특성을 조사하여 식품으로의 이용 가능성을 검토하고자 하였다. 선인장과 알로에의 주성분은 가용성 무질소물이었다. 총무기질 함량은 선인장 줄기, 열매와 씨가 각각 9400.8, 6151.2와 1096.8 mg%이며, 주요 무기질은 Ca, P, Mg이었다. 주요 유리 아미노산은 선인장 열매인 경우 tyrosine, proline과 arginine이, 줄기는 glycine과 arginine이 씨의 경우 glutamic acid이었다. 총 아미노산중 주요 아미노산은 열매의 경우는 glutamic acid가, 줄기는 glycine과 arginine이었으며, 씨는 glutmic acid와 arginine이었다. 비타민 C는 열매와 줄기가 각각 163.8과 71.2 mg% 존재하나 씨에는 존재하지 않았으며, 비타민 A는 모든시료에서 검출되지 않았다. 총 폴리페놀 화합물과 플라보노이드 함량은 추출방법에 따라 다르며, 총 폴리페놀 화합물의 경우 선인장 열매가 줄기와 씨보다 함량이 높았으며, 총 플라보노이드 함량은 줄기와 열매에서 비슷하였다.

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Neurospora crassa로부터 arginine transporter의 순수분리 (Purification of the Vacuolar Arginine Transporter from Neurospora crassa)

  • 이연희
    • 미생물학회지
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    • 제27권2호
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    • pp.117-123
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    • 1989
  • Radioactive NBZ arginyl diazomethane으로 액포를 표지 한 뒤에ㅣ 액포내의 단백질과 세포막 겉에 존재하는 단백질을 각각 저농도 완충용액과 높은 농도의 염용액으로 제거시켰다. 액포막 단백질을 Triton X-100으로 녹인 후, molecular sieve column chromatography와 ion exchange column chromatography를 사용하여 anginine transporter를 분리하였다.

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Effect of Ginsenoside on Basal and Nitro-L-Arginine Suppressed Nitric Oxide Production in Rat Kidney

  • Kim, Hye-Young;Han, Sang-Won
    • Biomolecules & Therapeutics
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    • 제2권2호
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    • pp.131-135
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    • 1994
  • The effect of ginsenoside (GS) from Panax ginseng on basal and nitro-L-arginine suppressed nitric oxide (NO) production was studied in rat kidney. NO production was determined by conversion to [$^{14C}$]=L-citrulline from [$^{14C}$]-L-arginine both in whole kidney and three renal segments; glomerulus, cortex excluding glomerulus (cortex-) and medulla. Nitro-L-arginine (total dose of 30 mg/kg/3 days, i.p.) significantly reduced NO production in whole kidney, which was prevented by GS pretreatment (30 mg/kg/3 days, i.p.). Relative high dose of GS (120 mg/kg/4 days, i.p..) selectively increased NO production in glomerulus and cortex-. Protein content, on wet weight basis, in cortex- and glomerular DNA content were significantly reduced by GS. Our results confirm the existence of constitutive nitric oxide synthase in kidney and it seems that target nephron segment for volume expansion due to GS'NO-mediated vasodilation and for NO production stimulated by GS is cortex including glomerulus.lus.

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$M_1$ Muscarine성 수용체에서 $^{123}Arginine$ 잔기의 Site-mutagenesis가 신호전달계에 미치는 영향 (Effects Of Site-mutagenesis of $^{123}Arginine$ residue in $M_1$ Muscarinic Receptor on the Signal Transduction System)

  • 이석용
    • 약학회지
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    • 제44권1호
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    • pp.52-59
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    • 2000
  • An exceptionally conserved sequence that is shared among most G protein-coupled neurotransmitter receptors is an aspartate-arginine-tyrosine triplet that is located at the second cytoplasmic domain. Using the ml subtype of muscarinic acetylcholine receptors as an example, a point mutation of the arginine residue at position 123 into asparagine was induced. This mutation resulted in a complete blockade of the carbachol-induced increases of PI hydrolysis and intracellular $Ca^2$$^{+}$ level, in spite of the expression of the wild-type and mutant receptors at similar concentrations in Chinese hamster ovary cells. In marked contrast, the muscarinic agonist carbachol induced concentration-dependent enhancement of the activity of NO synthase at mutant ml receptors although the enhancement was significantly smaller than at wild-type ml receptors. These data suggest that this highly conserved arginine residue plays an important role in coupling of muscarinic receptors to the second messenger systems and the presence of alternate mechanisms of activation of neuronal NO synthase which might be operative in the absence of large changes in the concentration of cellular $Ca^{2+}$.2+/.

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