• Asian-Australasian Journal of Animal Sciences
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• v.19 no.8
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• pp.1159-1163
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• 2006

This experiment was performed to examine the influences of high ambient temperature on milk production, nutrient digestibility, energy and protein sufficiency ratio, and plasma metabolites concentration in lactating cows. In a $2{\times}2$ crossover design, four multiparous lactating Holstein cows were maintained in a chamber under treatment of constant moderate ($18^{\circ}C$) ambient temperature (MT) or high ($28^{\circ}C$) ambient temperatures (HT). The DMI and milk protein yield were significantly lower in HT (p<0.05). The milk yield, milk lactose yield, and milk SNF yield tended to be lower in HT (p<0.10). No statistical differences for 4% fat-corrected milk and milk fat yield were observed. Rectal temperatures were significantly higher in HT than MT (p<0.05). The apparent DM, OM, ether extract, CF, and ash digestibility did not differ between treatments. On the other hand, the apparent CP digestibility was increased significantly (p<0.05) and nitrogen free extract tended to increase (p<0.10) in HT. The sufficiency ratio of ME and DCP intake for each requirement tended to be lower in HT than in MT (p<0.10). Concentrations of total protein (TP), albumin, and urea nitrogen in plasma did not differ between treatments. Plasma 3-methylhistidine (3MH) concentration as a marker of myofibrillar protein degradation tended to be higher in HT (p<0.15). In conclusion, high ambient temperature was associated with a lower energy and protein sufficiency ratio, and decreased milk protein production, even though the body protein mobilization tended to be higher.

• Applied Biological Chemistry
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• v.28 no.2
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• pp.88-91
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• 1985

For the systematic investigation of biochemical characteristics of Korean ginseng protein, protein fractions were analyzed by the techniques of sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The effect of pH and various salts on extractibility of ginseng protein were determined while the amino acid composition was studied by amino acid autoanalyzer. The protein was consisted of 66.08% of albumin and 20.51% of glutelin. Extractability of ginseng protein was the lowest in pH 3.0 and the highest in $pH\;6.0{\sim}8.0$. Among the neutral salts solution, $0.4M\;Na_2CO_3$ showed maximum extractability while $1.0M\;MgSO_4$ solution showed the least extractability. Resonable precipitation was obtained by 40% of acetone and ammonium sulfate. It has been shown by SDS polyacrylamide gel electrophoresis that the soluble protein had 11 bands. The molecular weight for the main protein of the soluble protein wasestimated to be 43,000. In amino acid composition of water extracted protein, arginine content was the highest 47.17% while on the contray, proline and cystine contents were very low.

• Journal of Microbiology and Biotechnology
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• v.11 no.4
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• pp.724-726
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• 2001

The growth of baceriophage T4 is inhibited by the presence of the tin gene product o bacteriophage P2. The interaction between purified Tin and gp32 proteins was observed using coimmunoprecipitation experiments. The in vivo interaction was confirmed by yeast two-hybrid experiments. A deletion analysis showed that the Asp 163 region of gp32 to DNA substrates was not affected by the presence of Tin, Thus, it would appear that the inhibition of 4 growth by Tin was due to a protein-protein interaction rather than affecting the DNA-binding ability of gp32.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.4
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• pp.536-542
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• 2007

The responses of whole body protein and glucose kinetics and of nitrogen (N) metabolism to non-protein energy intake (NPEI) were determined using an isotope dilution approach and measurement of N balance in three adult male goats. The diets containing 1.0, 1.5 and 2.0 times ME maintenance requirement, with fixed intake of CP (1.5 times maintenance) and percentage of hay (33%), were fed twice daily for each 21 d experimental period. After an adaptation period of 11 d, N balance was determined over 3 d. On day 17, whole body protein synthesis (WBPS) and glucose irreversible loss rate (ILR) were determined during the absorptive state by a primed-continuous infusion of [$^2H_5$]phenylalanine, [$^2H_2$]tyrosine, [$^2H_4$]tyrosine and [$^{13}C_6$]glucose, with simultaneous measurements of plasma concentrations of metabolites and insulin. Ruminal characteristics were also measured at 6 h after feeding over 3 d. Nitrogen retention tended to increase (p<0.10) with increasing NPEI, although digestible N decreased linearly (p<0.05). Increasing NPEI decreased (p<0.01) ammonia N concentration, but increased acetate (p<0.05) and propionate (p<0.05) concentrations in the rumen. Despite decreased plasma urea N concentration (p<0.01), increased plasma tyrosine concentration (p<0.05), and trends toward increased plasma total amino N (p<0.10) and phenylalanine concentrations (p<0.10) were found in response to increasing NPEI. Increasing NPEI increased ILR of both glucose (p<0.01) and phenylalanine (p<0.05), but did not affect ($p{\geq}0.10$) that of tyrosine. Whole body protein synthesis increased (p<0.05) in response to increasing NPEI, resulting from increased utilization rate for protein synthesis (p<0.05) and unchanged hydroxylation rate of phenylalanine ($p{\geq}0.10$). These results suggest that increasing NPEI may enhance WBPS and glucose turnover at the absorptive state and improve the efficiency of digestible N retention in goats, with possibly decreased ammonia and increased amino acid absorption. In addition, simultaneous increases in WBPS and glucose ILR suggest stimulatory effect of glucose availability on WBPS, especially when sufficient amino acid is supplied.

• Journal of Life Science
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• v.8 no.4
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• pp.400-409
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• 1998

Formation of adduct was studied in benzo(a)pyrene(BP)- and doxorubicin(Dx)-treated human NC-37 cells and isolated nuclei. Major adducts formed were determined by fluorescence absorption spectrophotometery and DNA-lin-ked protein assay. When isolated nuclei were exposed to carcinogens BP and DMBA, and anticancer drugs m-AMSA, ellipticine and Dx, varying degrees of adduct formation occured between DNA-protein complex and these drugs. When the mixture was centrifuged 1.7 M sucrose solution, binding BP and DMBA appeared to be similar between the sediment and the supernatant. When the sediment was centrifuged again with 0.35% polymin-P, the amount of BP bound was 2-fold greater in the protein(1077$\pm$55cpm) than in DNA fraction (470$\pm$20cpm), whereas that of DMBA was 1.6-fold greater in the DNA than in protein fraction. In the case of m-AMSA, ellipticine and Dx, the amount of binding was slightly greater in supernatant than in sediment in centrifugation with 1.7 M sucrose, and more than 3 times greater in the DNA- than in protein- fraction in centrifugation with 0.35% polymin P. DNA fractions which associated with a subset of nonhistone chromosomal protein were isolated from NC-37 cells exposed to $^{3}$H-BP and $^{14}$C-Dx. They were separated into two distince components DNA-S and DNA-P by centrifugation with 2M Nacl chromatin extraction. The results indicated that the amount of $^{3}$H-BP bound was 6.0-fold greater in DNA-P as compared with DNA-S, while that of $^{14}$C-Dx binding appreaed to be 6.2-fold greater in DNA-S than in DNA-P fraction. When $^{3}$H-BP binding wasdetermined in the presence of cold Dx, the amount of binding was reduced only in the DNA-P fraction, indicating that the interaction between DNA and protein is decreased. Gene expression by these drugs, BP treated cells were increased to compare with nomal cells but reduced by treatment with BP-Dx. These results suggest that the protein moiety which tightly bound to DNA-P fraction may play an important role in the regulation of gene expression.

• Archives of Pharmacal Research
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• v.4 no.2
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• pp.99-107
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• 1981

To investigate the protein binding characteristics of ibuprofenlysine, the effects of drub conentration, pH, ionic strength and protein concentration on the binding of drug to protein concentration on the binding of drug to protein were studied by fluorescence probe method. The conformational change of protein was investigated by circular dichroism (CD) measurement. As the concentration of drug increases, the association constant decreases. These may be due to complex formation of the probe and drug, or the interaction of the protein-probe complex and drug. The association constant for ibuprofenlysine increased with increasing protein concentration. These finding suggest a sharing of one ibuprofenlysine molecule by more than one protein molecule in the binding. The binding between ibuprofenlysine and protein was dependent on pH and ionic strength. It seems that both hydrophobic binding and some electrostatic forces are involved in the binding of ibuprofenlysing to protein.

• Asian-Australasian Journal of Animal Sciences
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• v.15 no.2
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• pp.222-237
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• 2002

Effects of high and low levels of feeding with or without protected protein on the performance of lactating goats were studied. Twenty four German Fawn goats either from 1st ($43.37{\pm}3.937$ kg and 2 year old) or 3rd $62.64{\pm}6.783$ kg and 4-5 year old) parity were used for the trial. Feeding levels were 7.2 (I) and 5.2 (II) MJ ME/litre of milk of 3.5% fat in addition to that of the maintenance allowance. At each feeding level, diet had either unprotected (U) or formaldehyde protected (P) soya-meal. Thus, four diets were IU, IP, IIU and IIP, having six animals in each. The diets were composed of hay and pellet (10:4:1 of beet pulp : barley : soya-meal). Effect of feeding level, protein protection, parity, health status and kid number on intake, milk yield, milk composition, growth rate of goats were recorded across the 21 weeks of study. High feeding level resulted increase (p<0.001) in estimated metabolizable energy (ME) and metabolizable protein (MP) availability. Dietary inclusion of protected soya-meal increased (p<0.001) the estimated MP but not the ME availability. Animals in 1st parity ate more (p<0.001) DM (111 vs. 102 g/kg $W^{0.75}$/d) than those in 3rd parity. Animals with twin kids (110 g/kg $W^{0.75}$/d) had higher (p<0.001) DM intake than those with single kid (102 g/kg $W^{0.75}$/d). Fat (4%) corrected milk (FCM) yield was not effected by high (1,924 g/d) or low (1,927 g/d) feeding level but increased (p<0.001) with protected (2,166 g/d) compared with unprotected (1,703 g/d) soya-meal. FCM yield for four dietary combinations were 1,806, 2,078, 1,600 and 2,254 g/d for diets IU, IP, IIU and IIP, respectively. For unit increase (g) in estimated MP availability relative to ME (MJ) intake, FCM yield increased ($1,418{\pm}275.6$) g daily ($r^2$=0.58; p<0.001). Milk fat (3.14 vs. 3.54%; p<0.001) and protein (2.94 vs. 3.04% p<0.05) contents were lower at high than the low feeding level. Protected protein increased (p<0.001) the fat, lactose and net energy (NE) content of milk. Milk urea concentration of 175, 183, 192 and 204 mg/l for diets IU, IP, IIU and IIP, respectively indicated lower RDP content of these diets. The RDP contents were 6.97, 6.70, 7.30 and 6.83 g/MJ of ME for diets IU, IP, IIU and IIP, respectively. Live weight change over the experimental period were 41, 6, 17 and 19 g/d. Absence of any positive response of high feeding was probably due to inefficient rumen fermentation resulting from inadequate RDP supply. Protected protein improved production performance apparently by increasing MP:ME ratio in the absorbed nutrient.

• BMB Reports
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• v.30 no.3
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• pp.222-228
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• 1997

Protein phosphatase 2C (PP2C) is one of the four major serine/threonine phosphatases which is dependent on $Mg^{2+}$ for its activity. PP2C was purified from rat liver cytosol and its characteristics were investigated. The substrate employed for routine assay was $[^{32}P]casein$ phosphorylated by PKA. The purification process involved DEAE chromatography, ammonium sulfate fractionation, phenyl sepharose chromatography, sephacryl 5-200 gel filtration, and histone agarose chromatography. The SDS-PAGE of PP2C showed one major single protein band at a position corresponding to a molecular mass of 43 kd and the purification fold was 637. The enzyme showed a pH optimum of 8 and $K_M$ value was $1.9\;{\mu}M$. However, when the substrate was changed to $[^{32}P]histone$, the pH optimum was shifted to 7 and $K_M$ value was $2.3\;{\mu}M.\;Mg^{2+}$ was essential to the enzyme activity and okadaic acid did not exert any inhibitory effect on the enzyme. To examine residue in the active site of PP2C effects of some protein-modifying reagents were tested.

• The Korean Journal of Food And Nutrition
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• v.9 no.3
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• pp.325-330
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• 1996

Foaming capacity (FC) and stability (FS) of protein recovered from red crab (Chitinonecetes opilio) processing in water and soybean protein isolate were determined at pH 2.0~10.0 in water and NaCl solution. The FC values for both proteins showed the lowest values at the isoelectric point (pH 4.0) and increased nth an increase in pH above the isoelectric point. FC of RCP was higher than that of SPI at pH 10.0 in water and both NaCl solutions. FC of SPI increased with an increase in NaCl concentration at pH 4.0 and 6.0, but FC of RCP was not affected. The highest FS values for both proteins were obtained at pH 4.0 in water. At pH 2.0, FC of RCP decreased with NaCl concentration increase, but FS increased. NaCl concentration had little effect on FS of RCP at pH 4.0 and 6.0, but the FS decreased at pH 10.0. FS of SPI was similar to that of RCP at pH 2.0 and increased with NaCl concentration Increase from 0.1 to 0.5M NaCl at pH 10.0.

• Food Science and Biotechnology
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• v.18 no.2
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• pp.396-401
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• 2009

The nucleotide sequence contains 2 open reading frames encoding a 45-amino-acid protein homologous to a transcriptional repressor protein CopG, and a 203-amino-acid protein homologous to a replication protein RepB. Putative countertranscribed RNA, a double-strand origin, and a single-strand origin were also identified. A shuttle vector, pUCL2.1, for various lactic acid bacteria (LAB) was constructed on the basis of the pCL2.1 replicon, into which an erythromycin-resistance gene as a marker and Escherichia coli ColE1 replication origin were inserted. pUCL2.1 was introduced into E. coli, Lc. lactis, Lactobacillus (Lb.) plantarum, Lb. paraplantarum, and Leuconostoc mesenteroides. The recombinant LAB maintained traits of transformed plasmid in the absence of selection pressure over 40 generations. Therefore, pUCL2.1 could be used as an E. coli/LAB shuttle vector, which is an essential to engineer recombinant LAB strains that are useful for food fermentations.