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Influence of polyphosphates on the emulsifying capacity of milk and meat proteinsCummins, Armando 27 August 1974 (has links)
The influence of polyphosphates upon the emulsification of
enzymatic hydrolyzates of casein and lactalbumin and upon salt-soluble
meat proteins was determined by a model system in which
oil-in-water emulsions were formed.
Sodium acid pyrophosphate, sodium tripolyphosphate and
sodium hexametaphosphate were mixed together in a weight ratio
of 4:2:4, respectively, to form a polyphosphate blend. This blend
was added at a level of 0.5% (w/v) to casein or lactalbumin dissolved
in 3% NaCl, pH 6.0. The polyphosphate blend was also added at the
above level to meat proteins solubilized in 3% NaCl, pH 5.7.
Emulsified volume (EV), total g of oil emulsified per 25 ml of protein
solution, was determined for the above proteins with or without
polyphosphates at varying protein concentrations. Data were also graphically expressed as emulsifying capacity (EC) and oil phase volume (OPV).
For all proteins studied with or without polyphosphates, EV
and OPV values increased with increasing protein concentration
whereas EC values decreased.
Addition of the polyphosphate blend to casein solutions containing
protein levels in excess of 2 mg/ml resulted in significantly
(P<0.01) higher EV levels than those of the controls. Conversely,
the EV values of the polyphosphate-treated lactalbumin solutions
were significantly (P< 0.01) lower than those of the controls at all
protein levels tested. The diverse data obtained with these two
proteins appear to be related to variations in molecular size and
shape and to differences in the manner in which the proteinphosphate
interactions occurred to cause the polyphosphates to
enhance the emulsification of casein while depressing that of lactalbumin.
Addition of the polyphosphate blend had little or no effect upon
the emulsification of meat protein extracts obtained from fresh,
frozen or refrozen samples. Thus, it was concluded that the polyphosphate
blend did not modify nor exert any detectable influence
upon the emulsification of solubilized meat proteins as tested in a
model system. / Graduation date: 1975
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A chromatographic method for estimating hydrophobic and electrostatic surface properties of soluble proteinsWijewickreme, Arosha Nilmini January 1990 (has links)
In this research experiments were carried out to estimate hydrophobic and electrostatic interactions in soluble proteins. Five proteins, lysozyme, lactalbumin, ovalbumin, myoglobin and ribonuclease-A were chromatographed isocratically on a HIC column at several molalities (0.3-1.3m) of each of three different neutral salts, ferrous sulfate, ammonium sulfate and sodium sulfate. The calculated retention coefficients were then fitted to a recently developed chromatographic model in two ways. a) Multiple regression analysis was conducted to estimate C values according to the non-linear model (log k = A + B log m + C m) . b) Simple regression analysis was conducted to estimate C′ values according to the linear model (log k = A′ + C′m) at higher salt concentrations (above 0.3m). Results indicated that C′ values better estimate the hydrophobic interactions than C values, in experiments conducted only at higher salt concentrations.
The comparison of C and C′ values with ANS, CPA, and Bigelow's average hydrophobicity indices showed no clear correlations. But, omission of ovalbumin improved the correlation coefficient of C′ with ANS. Both parameters indicated straight line relationships with molal surface tension increment of salts.
Further, the same model was used to estimate the
hydrophobic and electrostatic interactions in protein-protein interactions. Lysozyme and avidin were chromatographed on a lysozyme immobilized affinity column. Lysozyme-lysozyme interaction showed more affinity for hydrophobic interactions at low pH values. Avidin-lysozyme interaction showed both hydrophophobic and electrostatic interactions. Both interactions showed a greater change in the strength of hydrophobic interaction rather than the surface area of interaction, to changing pH. / Land and Food Systems, Faculty of / Graduate
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Biochemical study on the proteins of corn pollenOrtega, Enrique Ismael January 2011 (has links)
Digitized by Kansas Correctional Industries
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Biochemical characterization of the exuperantia protein in drosophila.January 1996 (has links)
by Pui-Ki Kwan. / Year shown on spine: 1997. / Thesis (M.Phil.)--Chinese University of Hong Kong, 1996. / Includes bibliographical references (leaves 134-143). / Acknowledgments --- p.i / Abstract --- p.ii / Abbreviations --- p.iii / Table of content --- p.v / Chapter CHAPTER 1 --- General Introduction / Chapter 1.1 --- The formation of body axes --- p.1 / Chapter 1.2 --- Maternal genes are essential for development --- p.8 / Chapter 1.3 --- Maternal gene bicoid is required for formation of anterior structures in the embryo --- p.9 / Chapter 1.4 --- Establishment of an anterior to posterior bcd protein gradient --- p.12 / Chapter 1.5 --- The bcd protein gradient regulates the downstream zygotic target genes in a concentration-dependent manner --- p.12 / Chapter 1.6 --- bcd protein acts as transcriptional regulators --- p.14 / Chapter 1.7 --- The anterior localization of bcd mRNA --- p.17 / Chapter 1.8 --- Components required for the localization of bcd mRNA --- p.17 / Chapter 1.8.1 --- Cis-acting elements --- p.17 / Chapter 1.8.1.1 --- BLE1 at 3' UTR directs localization of bcd mRNA --- p.19 / Chapter 1.8.2 --- Trans-acting elements --- p.21 / Chapter 1.8.2.1 --- "exuperantia, swallow and staufen are necessary for localization of bcd mRNA" --- p.21 / Chapter 1.8.2.2 --- exu protein is an absolute requirement for the localization --- p.24 / Chapter 1.8.2.3 --- Potential functions of exu based on the coding sequence --- p.25 / Chapter 1.8.2.4 --- Microtubules dependence of the localization --- p.26 / Chapter 1.8.2.5 --- Microtubules polarity directs localization of bcd RNAs --- p.27 / Chapter 1.9 --- Functions of exu in localization of bcd mRNA --- p.27 / Chapter CHAPTER 2 --- Characterization of deletion mutants of exu / Chapter 2.1 --- Introduction --- p.30 / Chapter 2.2 --- Construction of deletion mutants of exu --- p.31 / Chapter 2.2.1 --- Materials and Methods --- p.31 / Chapter 2.2.2 --- Results --- p.33 / Chapter 2.3 --- Analysis of exu protein in deletion mutants --- p.35 / Chapter 2.3.1 --- Materials and Methods --- p.35 / Chapter 2.3.1.1 --- Preparation of total ovary protein from the transgenic flies --- p.35 / Chapter 2.3.1.2 --- Analysis of protein content by SDS Polyacrylamide Gel Electrophoresis and immunoblotting --- p.35 / Chapter 2.3.2 --- Results --- p.36 / Chapter 2.4 --- Localization of bcd mRNA and exu protein in oogenesis --- p.39 / Chapter 2.4.1 --- Introduction --- p.39 / Chapter 2.4.2 --- Spatial and temporal distribution of exu protein in the deletion mutants --- p.41 / Chapter 2.4.2.1 --- Materials and Methods --- p.41 / Chapter 2.4.2.2 --- Results --- p.43 / Chapter 2.4.3 --- Spatial and temporal distribution of bcd mRNA in the deletion mutants --- p.56 / Chapter 2.4.3.1 --- Materials and Methods --- p.56 / Chapter 2.4.3.1.1 --- Principles of DIG-labeling and in situ hybridization --- p.56 / Chapter 2.4.3.1.2 --- Synthesis of DIG-labeled bcd DNA probe --- p.59 / Chapter 2.4.3.1.3 --- in situ hybridization of bcd mRNA in egg chambers using DIG-labeled DNA probe --- p.59 / Chapter 2.4.3.2 --- Results --- p.62 / Chapter 2.5 --- Discussion --- p.70 / Chapter CHAPTER 3 --- Determination of the interactions between exu and microtubules / Chapter 3.1 --- Introduction --- p.79 / Chapter 3.2 --- Localization of bcd mRNA and exu protein in the presence of drugs which destabilize cytoskeleton --- p.81 / Chapter 3.2.1 --- Materials and Methods --- p.81 / Chapter 3.2.2 --- Results --- p.82 / Chapter 3.3 --- Analysis of interactions between exu and microtubules by immunoprecipitation --- p.88 / Chapter 3.3.1 --- Materials and Methods --- p.88 / Chapter 3.3.1.1 --- Immunoprecipitation of exu protein and binding of microtubules --- p.88 / Chapter 3.3.1.2 --- Purification of tubulin from bovine or rat brains --- p.89 / Chapter 3.3.1.3 --- Determination of protein concentration of the tubulin stock by Folin-Lowry method --- p.90 / Chapter 3.3.1.4 --- Taxol-stabilized microtubules --- p.90 / Chapter 3.3.2 --- Results --- p.91 / Chapter 3.4 --- Analysis of interactions between exu and microtubules by cosedimentation --- p.94 / Chapter 3.4.1 --- Materials and Methods --- p.94 / Chapter 3.4.2 --- Results --- p.97 / Chapter 3.5 --- Analysis of interactions between exu and microtubules using detergent extracted ovary extract for co sedimentation --- p.100 / Chapter 3.5.1 --- Materials and Methods --- p.100 / Chapter 3.5.2 --- Results --- p.101 / Chapter 3.6 --- Analysis of intracellular distribution of exu protein and Release of exu protein by sodium carbonate treatment for cosedimentation with microtubules --- p.104 / Chapter 3.6.1 --- Materials and Methods --- p.104 / Chapter 3.6.1.1 --- Subcellular fractionation of ovary extracts --- p.104 / Chapter 3.6.1.2 --- Release of contents from fractions by sodium carbonate treatment --- p.105 / Chapter 3.6.1.3 --- Co sedimentation of exu protein with microtubules --- p.105 / Chapter 3.6.2 --- Results --- p.108 / Chapter 3.6.2.1 --- Intracellular distribution of exu protein --- p.108 / Chapter 3.6.2.2 --- Cosedimentation of exu protein with microtubules using Na2CO3 released extracts --- p.108 / Chapter 3.7 --- Cosedimentation of exu protein and microtubules in high ATP concentration --- p.113 / Chapter 3.7.1 --- Materials and Methods --- p.113 / Chapter 3.7.1.1 --- Preparation of ovary extracts and microtubules sedimentation --- p.113 / Chapter 3.7.1.2 --- Western blot using a chemiluminescent detection system --- p.114 / Chapter 3.7.2 --- Results --- p.115 / Chapter 3.8 --- Discussion --- p.122 / Chapter CHAPTER 4 --- Future Prospects --- p.125 / Appendix A Supplementary protocols --- p.126 / Appendix B Reagents --- p.131 / References --- p.134
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Biological and biochemical properties of crystalline and amorphous proteins from Phaseolus beansLi, Zhuo January 1992 (has links)
No description available.
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Low-molecular-weight subunits of glutelin in wheat and related species : their characterization, genetics and relation to bread-making qualityGupta, Ram Bilas. January 1989 (has links) (PDF)
Bibliography: leaves [133]-151.
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Purification and analysis of the trichohyalin gene : an examination of the role of tricohyalin in the inner root sheath / Michael James Fietz.Fietz, Michael J. January 1991 (has links)
Includes bibliographical references. / 1 v. ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.)--University of Adelaide, Dept. of Biochemistry, 1991
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Functional analysis of novel ��-catenin mutantsAl-Fageeh, Mohamed B. 12 February 2003 (has links)
��-catenin is a multi functional protein that is involved in cell-cell adhesion
and cell signaling. In non-stimulated cells, ��-catenin is tightly down-regulated by
GSK-3��-dependent phosphorylation at Ser and Thr residues, followed by rapid
ubiquitination and proteasomal degradation. It is well established that mutations
within the regulatory GSK-3�� region lead to stabilized ��-catenin and constitutive
��-catenin/TCF-dependent gene activation. Furthermore, it has been shown that
amino acids adjacent to codon 33, namely 32 and 34 of ��-catenin, are hotspots for
substitution mutations in carcinogen-induced animal tumors. Thus, a major
hypothesis of this thesis was that substitution mutations at codon 32 of ��-catenin
interfere with phosphorylation and ubiquitination of ��-catenin.
Site-directed mutagenesis was used to create defined ��-catenin mutants,
namely D32G, D32N, and D32Y. The signaling potential of various ��-catenin was
analyzed in a gene reporter assay by co-transfection with a hTcf cDNA with a
reporter plasmid containing a Tcf-dependent promoter (TOPFlash). There was a
significant enhancement of the reporter gene activity with all ��-catenin mutants
compared to WT ��-catenin after 48 hours of transfection. Protein analysis by
Western blotting showed massive accumulation of mutant ��-catenin. Antibody
specific for phosphorylated ��-catenin showed that the accumulated D32G and
D32N ��-catenin proteins were strongly phosphorylated both in vivo and in vitro,
whereas D32Y ��-catenin exhibited significantly attenuated phosphorylation in vivo.
Further studies showed, however, that none of the mutants was sufficiently
ubiquitinated. In addition, inhibition of the proteasome activity by ALLN was
associated with accumulation of cytosolic ��-catenin, which was transcriptionally
inactive. This suppression of ��-catenin transcriptional capacity was independent of
ALLN-associated apoptosis in the transfected cells. Furthermore, exogenous ��-catenin mediated modest cell survival and rendered cells sensitive to apoptotic stimuli.
Thus, although codon 32 of ��-catenin is not a direct target for
phosphorylation, results from this thesis suggested that it affects the
phosphorylation and ubiquitination of the adjacent Ser-33 residue of ��-catenin,
which is a direct target of GSK-3��. In addition, these results showed for the first
time that the phosphorylation step of ��-catenin is not enough to regulate
transcriptional activity, and that ��-catenin still needs to be ubiquitinated for
successful down-regulation. / Graduation date: 2003
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Structural characterization of the ribonuclease P protein aRpp29 from the hyperthermophilic sulfate-reducing Archaeon Archaeoglobus fulgidusSidote, David Joseph 28 August 2008 (has links)
Not available / text
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Computational methods in protein mass spectrometry, DNA microarray technology and protein foldingNakorchevskiy, Aleksey Alfred 28 August 2008 (has links)
Not available / text
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