• 제목/요약/키워드: p60 protein

검색결과 1,563건 처리시간 0.023초

Differential expression of heat shock protein 90, 70, 60 in chicken muscles postmortem and its relationship with meat quality

  • Zhang, Muhan;Wang, Daoying;Geng, Zhiming;Sun, Chong;Bian, Huan;Xu, Weimin;Zhu, Yongzhi;Li, Pengpeng
    • Asian-Australasian Journal of Animal Sciences
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    • 제30권1호
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    • pp.94-99
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    • 2017
  • Objective: The aim of this study was to investigate the expression of heat shock protein (HSP) 90, 70, and 60 in chicken muscles and their possible relationship with quality traits of meat. Methods: The breast muscles from one hundred broiler chickens were analyzed for drip loss and other quality parameters, and the levels of heat shock protein (HSP) 90, 70, and 60 were determined by immunoblots. Results: Based on the data, chicken breast muscles were segregated into low (drip loss${\leq}5%$), intermediate (5%${\geq}9.5$) drip loss groups. The expression of HSP90 and HSP60 were significantly lower in the high drip loss group compared to that in the low and intermediate drip loss group (p<0.05), while HSP70 was equivalent in abundance in all groups (p>0.05). Conclusion: Results of this study suggests that higher levels of HSP90 and HSP60 may be advantageous for maintenance of cell function and reduction of water loss, and they could act as potential indicator for better water holding capacity of meat.

Localization of Sop Proteins and Interaction of Plasmid DNA with the Cell Membrane of Host Bacteria in Partitioning

  • Kim, Sung-Uk;Nagai, Kazuo;Tamura, Gakuzo;Yu, Ju-Hyun
    • Journal of Microbiology and Biotechnology
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    • 제3권4호
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    • pp.261-265
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    • 1993
  • A sopA protein (41K) encoded by plasmid pXX288 was observed in the cytoplasm, whereas a sopB protein (37K) encoded by plasmid pXX157 was observed in the membrane fraction. Most of the sopB protein was solubilized from the crude membrane by treatment with Sarkosyl, which suggested that the protein may be located in the inner membrane. The sopA protein was precipitated at the concentration of 30 to 60% ammonium sulfate. The sedimentation profile of the crude membrane fraction showed a little difference according to culture media used, and the sopB protein existed in all fractions of inner membrane. The DNA of plasmids, pXX157, pXX300, and pXX167 co-sedimented with inner membrane fraction.

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모형식품의 열확산도에 관한 연구 (Studies On Thermal Diffusivity of Model Foods)

  • 장규섭;김동만;김재욱
    • 한국식품과학회지
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    • 제18권1호
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    • pp.24-30
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    • 1986
  • 전분, 단백질 및 수분으로 주로 구성된 한국의 일반 식품과 유사한 모형식품을 이들 세가지 주성분을 조합하여 만들었으며, 이 모형식품의 열확산도를 측정하고 주성분과의 관계를 구명하였다. 모형식품의 열확산도는 수분함량에 비례하는 경향이었고, 동일 수분함량에서는 전분질식품이 단백질 식품보다 높은 값을 나타냈으며 성분간의 교호작용은 유의석이 인정되지 않았다. 측정치와 계산치간의 오차는 잔여율이 3.60%로서 부함도가 높았다. 모형식품에서 열확산도와 수분함량, 단백질 및 전분함량과의 관계식은 다음과 같다. 즉, ${\alpha}20^{\circ}C$ = 0.04911M+0.37355P+3.73072, ${\alpha}60^{\circ}C$ = 0.05353M-0.4766P+4.15136, 이식을 이용한 산술치와 측정치간의 상관계수는 $20^{\circ}C$에서 $0.9650^{**}$, $60^{\circ}C$에서 $0.9002^{**}$로 고도의 유의 상관관계를 나타내었다.

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체강삼출액의 진단에 있어서 p53 단백의 유용성 (Diagnostic Value of p53 Expression in the Evaluation of Effusions)

  • 이지신;박창수
    • 대한세포병리학회지
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    • 제7권2호
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    • pp.138-143
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    • 1996
  • The diagnostic accuracy of routine cytological preparations from effusions ranges from 60% to 70%. Immunohistochemical markers, especially tumor-associated antigens, have been successfully employed to increase diagnostic sensitivity in effusion cytology. However, more than two different antibodies in diagnosis of effusions are needed. In the view of prevalence of abnormalities of p53 gene in human malignancies we investigated the diagnostic usefulness of demonstration of p53 protein immunoreactivity in distinguishing benign changes versus malignant processes in effusions. p53 protein expression was studied immunohistochemically in 76 effusions(28 malignant and 48 benign) using anti-human p53 antibody p53 immunoreactivity was identified in 19 of 28(67.9%) malignant effusions. In contrast, no p53 immunoreactivity was observed in all benign effusions. A specificity of 100% and a sensitivity of 67.9% were observed. These results suggest that immunohistochemical detection of p53 protein seems to be helpful in distinguishing benign changes versus malignant processes in effusions, although its principal limitation is its relatively low sensitivity.

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감귤과피 압착액을 기질로 한 SCP 생산 (SCP Production from Mandarin Orange Peel Press Liquor)

  • 강신권;성낙계
    • 한국미생물·생명공학회지
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    • 제17권6호
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    • pp.556-562
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    • 1989
  • The bioconversion of mandarin orange peel press liquor to single cell protein (SCP) by two yeast strains, F-60, and C-7, which were isolated from mandarin orange peel was carried out and compared with that of using Candida utilis IFO 0598. Experiments were directed toward the high yield of biomass and high protein in cultures of the strains mentioned above. Candida utilis IFO 0598, F-60 and C-7 strains were cultivated at 3$0^{\circ}C$, pH 5.2 for 3 days in shaking flasks. The effects of some nutrients on cell growth were studied. Cell mass and protein content per cell mass were increased by addition of urea 1%, KH$_2$PO$_4$ 0.1% and MgSO$_4$ㆍ7$H_2O$ 0.05%, When the F-60 strain cultured under the optimal conditions, cell mass, growth yield and protein content were 41.2g/l, 53.9%, 59.7%, respectively. Cell mass was also increased up to 15% by modifying the fermentation condition on the bench type 20l jar fermentor. Crude fat content (10.3%) of dried C-7 cell was higher than those of C. utilis and F-60, 4.9% and 5.6% respectively. Total protein content of the F-60 strain was 59.7% per dry weight. And we compared their amino acid compositions with that of FAO provisional pattern. In the case of the F-60 strains, amino acid contents such as lysine, leucine and isoleucine were much higher than those of methionine, cystine and tryptophan.

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치어기 잉어에 있어 사료내 단백질원으로서 어분대체품의 이용성 (Utilization of Fish Meal Analogue as a Dietary Protein Source in Fingering Common Carp, Cyprinus carpio)

  • 박흥식;배승철;김강웅;조재윤
    • 한국양식학회지
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    • 제12권2호
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    • pp.107-114
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    • 1999
  • This study was conducted to evaluate the possible utilization and the replacing range of fish meal analogue (FMA) as a dietary animal protein source for fish meal replacer in fingerling common carp, Cyprinus carpio. Leather meal, meat and bone meal, feather meal, squid liver powder, poultry by product meal, blood meal and amino acids were selected as ingredients for FMA. fish averaging 12.5 g were fed one of five isonitrogenous and isocaloric diets containing fish meal and/or FMA as the dietary animal protein sources. Fish meal protein (0, 20, 40, 60 or 100%) was replaced by the graded level of FMA protein. The feeding trial was conducted for 12 weeks after one week of conditioning period. Percent weight gain of fish fed diets containing 20%, 40% and 60% FMA were not significantly different from that of the fish fed the control diet (P>0.05). Feed conversion ratio of fish fed diets containing 20%, 40%, 60% and 100% FMA were not significantly different from that of fish fed control diet. These findings suggest that replacement of fish meal protein by FMA could be possible up to 60% of fish meal protein in fingerling Israeli carp diets.

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돌둠사료의 적정 단백질 및 지질 함량 (Optimum Dietary Protein and Lipid Levels on Growth in Parrot Fish (Oplegnathus fasciatus))

  • 강용진;이상민;황형규;배승철
    • 한국양식학회지
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    • 제11권1호
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    • pp.1-10
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    • 1998
  • 돌돔 사료의 적정 단백질 및 지질 함량을 구하기 위해 북양어분과 카제인을 단백원으로 하여 사료의 단백질 함량이 30, 40, 50 및 60%가 되도록 하고, 각 단백질 함량에 지질 함량이 8 및 16%가 되는 8종의 실험사료로 평균체중 7 g의 돌돔을 대상으로 8주간 사육 실험하였다. 사료의 단백질 함량에 따른 증체율 및 사료효율은 사료지질 8% 수준에서 사료단백질이 40% 이상인 사료구에서는 사료단백질 함량이 증가함에 따라 유의차 있게 증가하였으며(P<0.05), 사료지질 16% 수준에서는 사료단백질이 증가함에 따라 증가하다가, 사료단백질 50% 이상에서는 유의적인 차이가 없었다(P>0.05). 사료지질 16% 수준에서 broken line model을 이용하여 증체율을 지표로 하여 돌돔의 적정 단백질 요구량을 구한 결과 46%로 추정되었다. 사료의 지질 함량에 따른 증체율은 사료단백질 40 및 50% 수준에서 고지질 사료구(16%)가 유의하게 높았으며, 사료효율은 모든 사료단백질 수준에서 고지질 사료구(16%)가 유의하게 높았다(P<0.05). 단백질 효율 및 단백질 축적율은 모든 사료단백질 수준에서 고지질 사료구가 높았다. 따라서 성장과 사료효율을 기준으로 볼 때 돌돔 사료의 적정 지질 함량은 16% 전후로 추정되었다. 전어체 및 등근육의 성분에서 단백질은 사료의 단백질 함량이 증가함에 따라 증가하다가 사료 단백질 40% 이상에서는 유의차가 없었으며, 지질은 모든 사료단백질 수준에서 고지질 사료구가 높았다. 간 및 내장의 성분에서 단백질은 사료의 단백질 함량에 따라 뚜렷한 경향이 없었지만, 지질은 모든 사료단백질 수준에서 고지질 사료구(16%)가 높았다.

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Pepstatin- Insensitive Carboxyl Proteinase: A Biochemical Marker for Late Lysosomes in Amoeba proteus

  • Hae Kyung Kwon;HyeonJung Kim;Tae In Ahn
    • Animal cells and systems
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    • 제3권2호
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    • pp.221-228
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    • 1999
  • In order to find a biochemical marker for late Iysosomes, we characterized two cDNAs which were cloned by using a monoclonal antibody (mAb) against Iysosomes in Amoeba proteus as a probe. The two cDNAs, a 1.3-kb cDNA in pBSK-Iys45 and a 1.6-kb cDNA in pBSK-Iys60, were found to encode proteins homologous to pepstatin-insensitive carboxyl proteinases (PICPs). E. coli transformed with pBSK-Iys45 produced two immunopositive polypeptides (45 and 43 kDa) and the cDNA in 1274 bases encoded a 44,733-Da protein (Lys45) of 420 amino acids containing one site for a core oligosaccharide. On the other hand, E. coli transformed with pBSK-Iys60 produced several polypeptides (64, 54, 45, 41, and 37 kDa) reacting with the mAb. The cDNA contained 1629 bases and encoded a 59,231-Da protein (Lys60) of 530 amino acids containing two sites for asparagine-linked core oligosaccharides. These two cDNAs showed identities of 60.3% in nucleotide sequences and 23.6% in amino acid sequences. Lys45 and Lys60 appeared to share XXEFQK as a common antigenic domain. The amino acid sequence of the Lys45 protein showed 17.4% identity and 40.9% similarity to that of PICP from Pseudomonas sp. 101. On the other hand, Lys60 showed a 24.3% identity and 51.9% similarity with human Iysosomal PICP in the amino acid sequence. A putative active center for serine protease, GTS*xxxxxFxG, was found to be conserved among PICP homologues. The two PICPs are the first reported enzymatic markers for late Iysosomes.

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Protease 처리가 누에번데기 단백질 추출 및 기능성에 미치는 영향 (Effect of Protease on the Extraction and Properties of the Protein from Silkworm pupa)

  • 권효정;이경환;김정환;천성숙;조영제;차원섭
    • Applied Biological Chemistry
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    • 제49권4호
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    • pp.304-308
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    • 2006
  • 누에번데기에 함유되어 있는 불용성 단백질을 가용성 단백질로 추출시키기 위하여 누에번데기에 Bacillus sp. JH-209 균주로부터 생산된 protease를 작용시켰다. 이때 누에번데기 단백질의 추출을 위한 적정 pH는 pH $7{\sim}11$까지의 알칼리 영역에서 추출율의 증가를 보였다. 최적 온도는 $40^{\circ}C$였고, 최적 작용시간은 11시간이었고, 효소의 최적 첨가량은 60 unit 정도였다. 효소처리 된 누에번데기 단백질은 효소처리하지 않은 대조구에 비해 기포력, 기포안정성, 유화력과 유화안정성이 증가하였고, 유지흡착력과 수분흡착력도 대조구에 비해서 높은값을 나타내었다.

효소처리한 번데기 농축단백질의 기능적 특성 (Functional Properties of Silkworm Larvae Protein Concentrate After Enzyme Treatments)

  • 전정례;박정륭
    • 한국식품영양과학회지
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    • 제21권6호
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    • pp.706-711
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    • 1992
  • Papain과 pepsin에 의한 부분 가수분해가 번데기 농축단백질의 기능적 특성에 미치는 영향을 검토하였다. TCA 가용성 질소량을 측정하여 얻은 가수분해 정도는 papain으로 10분과 60분간 처리한 결과 각각 10.23%와 19.17% 였으며 pepsin으로 10분과 60분간 처리한 경우는 각각 15.41%와 21.41%로 나타났다. 효소처리한 번데기 농축단백질의 질소 용해도는 실험한 pH 전범위에서 증가하였으며 특히 papain과 pepsin 모두 60분 처리한것이 10분간 처리한것 보다 높게 나타났다. 0.03M $CaCl_2$를 첨가한 결과 전반적으로 질소 용해도가 증가하는 경향을 나타내었다. 번데기 농축단백질의 겉보기 밀도는 papain으로 처리시 차이가 나타나지 않았으며 pepsin의 겨우는 다소 증가하는 경향이었다. 수분 흡수력의 경우 pepsin으로 10분간처리한것 이외에는 큰차이를 나타내지 않았으나 지방흡수력은 papain과 pepsin으로 부분 가수분해한 결과 전반적으로 증가하였다.

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