Heat-Induced Redistribution of Disulfide Bonds in Milk Proteins. 2. Disulfide Bonding Patterns between Bovine β-Lactoglobulin and κ-Casein

2004 ◽  
Vol 52 (25) ◽  
pp. 7669-7680 ◽  
Author(s):  
Edwin K. Lowe ◽  
Skelte G. Anema ◽  
Annie Bienvenue ◽  
Michael J. Boland ◽  
Lawrence K. Creamer ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Milk Proteins ◽  
Disulfide Bonding ◽  
Β Lactoglobulin ◽  
Bonding Patterns

Heat-Induced Redistribution of Disulfide Bonds in Milk Proteins. 1. Bovine β-Lactoglobulin

2004 ◽  
Vol 52 (25) ◽  
pp. 7660-7668 ◽  
Author(s):  
Lawrence K. Creamer ◽  
Annie Bienvenue ◽  
Hanna Nilsson ◽  
Marie Paulsson ◽  
Miriam van Wanroij ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Milk Proteins ◽  
Β Lactoglobulin

Occurrence of milk proteins in the urine of cows during an extended milking interval

1967 ◽  
Vol 34 (1) ◽  
pp. 27-30 ◽  
Author(s):  
R. L. J. Lyster ◽  
J. V. Wheelock
Keyword(s):  
Molecular Weight ◽  
Milk Proteins ◽  
Immunological Methods ◽  
Factors Affecting ◽  
Β Lactoglobulin

SummaryImmunological methods have been used to test samples of urine from 5 cows for the presence of milk proteins. None could be detected when the cows were milked twice daily at the usual intervals, but during an extended milking interval α-lactalbumin was found in the urine of all 5 cows and β-lactoglobulin in the urine of 2 cows. The urine of one cow during and after a milking interval of 39 h contained 1·63 g α-lactalbumin, 1·12 g β-lactoglobulin and a small amount of casein. One of the factors affecting the transfer of these milk constituents from the udder to the urine appears to be their molecular weight.

Mass Spectrometric Based Mapping of the Disulfide Bonding Patterns of Integrin α Chains†

Biochemistry ◽  
2003 ◽  
Vol 42 (44) ◽  
pp. 12950-12959 ◽  
Author(s):  
Oleg V. Krokhin ◽  
Keding Cheng ◽  
Sandra L. Sousa ◽  
Werner Ens ◽  
Kenneth G. Standing ◽  
...  
Keyword(s):  
Mass Spectrometric ◽  
Disulfide Bonding ◽  
Bonding Patterns

Relationship between protein structures and disulfide-bonding patterns

2003 ◽  
Vol 53 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Chao-Chun Chuang ◽  
Chun-Yin Chen ◽  
Jinn-Moon Yang ◽  
Ping-Chiang Lyu ◽  
Jenn-Kang Hwang
Keyword(s):  
Protein Structures ◽  
Disulfide Bonding ◽  
Bonding Patterns

Attachment of Listeria innocua to Polystyrene: Effects of Ionic Strength and Conditioning Films from Culture Media and Milk Proteins

2014 ◽  
Vol 77 (3) ◽  
pp. 427-434 ◽  
Author(s):  
GILLES ROBITAILLE ◽  
SÉBASTIEN CHOINIÈRE ◽  
TIMOTHY ELLS ◽  
LOUISE DESCHÈNES ◽  
AKIER ASSANTA MAFU
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bacterial Adhesion ◽  
Bovine Serum ◽  
Biofilm Formation ◽  
Milk Protein ◽  
Milk Proteins ◽  
Listeria Innocua ◽  
Conditioning Films ◽  
Β Lactoglobulin

It is recognized that bacterial adhesion usually occurs on conditioning films made of organic macromolecules absorbed to abiotic surfaces. The objectives of this study were to determine the extent to which milk protein–coated polystyrene (PS) pegs interfere with biofilm formation and the synergistic effect of this conditioning and hypertonic growth media on the bacterial adhesion and biofilm formation of Listeria innocua, used as a nonpathogenic surrogate for Listeria monocytogenes. PS pegs were uncoated (bare PS) or individually coated with whey proteins isolate (WPI), β-lactoglobulin, bovine serum albumin, or tryptic soy broth (TSB) and were incubated in bacterial suspensions in modified Welshimer's broth. After 4 h, the number of adherent cells was dependent on the coating, as follows: TSB (107 CFU/ml) > bare PS > β-lactoglobulin > bovine serum albumin ≈ WPI (104 CFU/ml). The sessile cell counts increased up to 24 h, reaching >107 CFU per peg for all surfaces (P > 0.1), except for WPI-coated PS; this indicates that the inhibitory effects of milk protein conditioning films are transient, slowing down the adhesion process. The 4-h bacterial adhesion on milk protein–coated PS in modified Welshimer's broth supplemented with salt (0 to 10% [wt/vol]) did not vary (P > 0.1), indicating that conditioning with milk proteins was the major determinant for inhibition of bacterial adhesion and that the synergetic effect of salt and milk proteins on adhesion was minimal. Moreover, the presence of 5 to 10% salt significantly inhibited 24-h biofilm formation on the TSB-coated and bare PS, with a decrease of >3 log at 10% (wt/vol) NaCl and almost completely depleted viable sessile bacteria on the milk protein–coated PS.

scholarly journals Development and Validation of a Method for the Quantification of Milk Proteins in Food Products Based on Liquid Chromatography with Mass Spectrometric Detection

2011 ◽  
Vol 94 (4) ◽  
pp. 1043-1059 ◽  
Author(s):  
Petra Lutter ◽  
Véronique Parisod ◽  
Hans Weymuth
Keyword(s):  
Milk Powder ◽  
Skim Milk ◽  
Internal Standard ◽  
Milk Proteins ◽  
Skim Milk Powder ◽  
Selected Reaction Monitoring ◽  
Validation Data ◽  
Development And Validation ◽  
Protein Rich ◽  
Β Lactoglobulin

Abstract The protection of allergic consumers is crucial to the food industry. Therefore, accurate methods for the detection of food allergens are required. Targeted detection of selected molecules by MS combines high selectivity with accurate quantifcation. A confrmatory method based on LC/selected reaction monitoring (SRM)-MS/MS was established and validated for the quantifcation of milk traces in food. Tryptic peptides of the major milk proteins β-lactoglobulin, β-casein, αS2-casein, and κ-casein were selected as quantitative markers. Precise quantifcation was achieved using internal standard peptides containing isotopically labeled amino acids. For each peptide, qualifer and quantifer fragments were selected according to Commission Decision 2002/657/EC. A simple sample preparation method was established without immunoaffnity or SPE enrichment steps for food matrixes containing different amounts of protein, such as baby food, breakfast cereals, infant formula, and cereals. Intermediate reproducibility, repeatability, accuracy, and measurement uncertainty were determined for each matrix. LOD values of 0.2–0.5 mg/kg, e.g., for β-lactoglobulin, were comparable to those obtained with ELISA kits. An LOQ of approximately 5 mg/kg, expressed as mass fraction skim milk powder, was validated in protein-rich infant cereals. The obtained validation data show that the described LC/SRM-MS/MS approach can serve as a confrmatory method for the determination of milk traces in selected food matrixes.

β-Lactoglobulin Self-Assembly: Structural Changes in Early Stages and Disulfide Bonding in Fibrils

2013 ◽  
Vol 61 (32) ◽  
pp. 7817-7828 ◽  
Author(s):  
Anant C. Dave ◽  
Simon M. Loveday ◽  
Skelte G. Anema ◽  
Trevor S. Loo ◽  
Gillian E. Norris ◽  
...  
Keyword(s):  
Self Assembly ◽  
Structural Changes ◽  
Disulfide Bonding ◽  
Early Stages ◽  
Β Lactoglobulin

scholarly journals Bovine antibodies with ultra long H3 Complementarity Determining Regions

2014 ◽  
Vol 70 (a1) ◽  
pp. C255-C255
Author(s):  
Robyn Stanfield ◽  
Vaughn Smider ◽  
Ian Wilson
Keyword(s):  
Disulfide Bonds ◽  
The Other ◽  
Sequence Length ◽  
Antibody Repertoire ◽  
Human Antibody ◽  
Structural Homology ◽  
Disulfide Bonding ◽  
Cysteine Rich Protein ◽  
Complementarity Determining Regions ◽  
Bovine Antibody

About 10% of the bovine antibody repertoire exhibit extremely long H3 complementarity determining regions (CDRs). These H3 CDRs are usually described as `loops' in the more familiar mouse and human antibody Fab structures, but the ultra long bovine H3 CDRs are actually small, cysteine-rich protein domains that vary in size from 44 to 64 amino acids. We have recently determined the structures for two bovine antibody Fab fragments, and will describe these, as well as compare them with two other previously determined bovine Fab structures (Wang et al., Cell, 2013). One new Fab has a relatively short H3 CDR region of 44 residues, with just one disulfide bond, while the other boasts one of the longest H3 CDRs, with 63 residues and four disulfide bonds. These H3 CDRs fold to form apparently rigid `stem' regions, that present the disulfide bonded `knob' domain far above the five other Fab CDR loops. Despite extreme diversity in sequence, length and disulfide bonding patterns, the CDRs share structural homology, both in their long stems and in the more variable knob regions.

Heat-induced interactions of β-lactoglobulin A and κ-casein B in a model system

2003 ◽  
Vol 70 (1) ◽  
pp. 61-71 ◽  
Author(s):  
Younghee Cho ◽  
Harjinder Singh ◽  
Lawrence K Creamer
Keyword(s):  
Heat Stability ◽  
Model System ◽  
Hydrophobic Association ◽  
Milk Product ◽  
Disulphide Bonds ◽  
Sds Page ◽  
Β Lactoglobulin ◽  
Circular Dichroïsm ◽  
Product Functionality ◽  
Bonding Patterns

The interaction of κ-casein and β-lactoglobulin is fundamental to all heat-induced modifications of milk product functionality, such as the heat stability of concentrated milks. Purified native κ-casein B and β-lg A solutions were heated at 80 °C at pH 6·7 separately and in a mixture. The circular dichroism spectra in the near UV indicated irreversible changes in the disulphide bonding patterns involving both proteins. Alkaline- and SDS-PAGE of heated samples showed that, in the presence of κ-casein, less β-lg was converted into β-lg polymers and the rate of loss of native β-lg was greater. When κ-casein was added to previously heated β-lg and the mixture was heated, the κ-casein reacted with the heat-induced β-lg polymers more readily than with the β-lg native monomers. The formation of β-lg dimers, trimers etc. was diminished. It was concluded that, when β-lg and κ-casein were heated together, β-lg formed thiol-exposed monomers, which reacted with each other or with the native κ-casein depending on the relative concentrations of β-lg and κ-casein. The products of these reactions included some disulphide-bonded 1[ratio ]1 β-lg[ratio ]κ-casein complexes, some monomer κ-casein and a range of large aggregates held together by either or both disulphide bonds and hydrophobic association.

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