Advanced Dairy Chemistry

Index 541 centrifugation after calcium enrichment, 47 Chromatin, 440–441 cryoprecipitation, 48 Chronic hepatitis C (CHC), 303 ethanol precipitation, 48 CID. See Collision-induced dissociation (CID) gel filtration, 48 CIFN. See Consensus interferon (CIFN) isoelectric precipitation, 46–47 Circular dichroism (CD), 111–112, 169 membrane filtration, 47–48 CIS. See Crystalline insoluble substance (CIS) rennet coagulation, 48 CMP. See Caseinomacropeptide (CMP) salting-out methods, 47 CMV. See Cytomegalovirus (CMV) ultracentrifugation, 47 Cobalamin, 325 Caseins Collision-induced dissociation (CID), 108 as1-casein, 392 Colloidal calcium phosphate (CCP), 46 as2-casein, 395–397 Colostrum b-casein milk immunoglobulins amino acid sequence, 394 intestinal actions, 283–284 exon skipping, 395 nutritional value, 284–285 gene encoding, 395 casein gene locus, 389–392 role of, 285 comparison with whey proteins Column chromatography amino acid composition, 49–50 biosynthesis site, 50 gel filtration, 101–102 coagulation by limited proteolysis, 49 hydrophobic interaction and reversed-phase heat stability, 49 physical state, 50 (RP)-HPLC, 104–105 solubility at pH 4.6, 49 ion exchange, 102–104 functions of, 161 Consensus interferon (CIFN), 303 heterogeneity and fractionation, 50–53 Conversion factors, quantitation, 89–90 interspecies comparison, 74–75 Crocidura russula, 2 k-casein, 397 Cryoprecipitation, 48 micelle model, 388 Crystalline insoluble substance (CIS), 58 micelle organisation, 404–405 Cytomegalovirus (CMV), 303 microheterogeneity, 54–56 CZE. See Capillary zone electrophoresis (CZE) molecular modeling as1-casein, 165–168 D as2-casein, 173–174 Dietary proteins b-casein, 168–170 k-casein, 170–173 amino acid requirements, 517–518 mixed associations, 174–175 protein digestibility, 519–520 sodium caseinate, 176–179 protein requirements, 516–517 post-translational modifications protein utilisation, 520–521 glycosylation, 404 Disulfide bonding, 55 phosphorylation, 402–403 Dual-bonding model, casein micelle, 73 post-translational process, 389 pre-mammalian origin, 14 E protein structure EGF. See Epidermal growth factor (EGF) classification, 165 Egg-white lysozyme (EWL), 364–367 IUP/NU, 163 Electron micrographs (EM), 176 PMG, 163, 164 Electrophoresis properties, 163 SAA deficit, 27 capillary, 101 secretory calcium-binding phosphoproteins, 14–18 isoelectric focusing, 100–101 splice variants microfluidic “lab-on-a-chip” techniques, 101 cryptic splice sites, 399 milk proteins applications, 53–54 genetic polymorphism, 400–401 native, 99 “species-specific” casual exon skipping, 399–400 SDS, 99–100 tensegrity hypothesis and resolution, 179–182 two-dimensional, 101 three-dimensional molecular models, 163 Electrospray ionisation mass spectrometry (ESI-MS), vitellogenins, 18 Catalase, indigenous enzymes, 341–342 106–107 CCP. See Colloidal calcium phosphate (CCP) ELISA. See Enzyme-linked immunosorbent assay (ELISA) CE. See Capillary electrophoresis (CE) EM. See Electron micrographs (EM) CHC. See Chronic hepatitis C (CHC) Enzyme-linked immunosorbent assay (ELISA) accuracy and precision, 116 advantages, 115 BSA, 118 a-lactalbumin, 118

542 Index Enzyme-linked immunosorbent assay (ELISA) (cont.) MFGE8, 494–495 lactoferrin, 118–119 MUC-1, 491, 493 b-lactoglobulin, 117–118 protein-encoding gene, 496 plasmin, 119 molecular basis, 466–467 sensitivity, definition of, 116 g-Glutamyl transferase (GGT), 347–348 types of, 115 Glutathione peroxidase (GSHPOx), 347 Glycomacropeptide (GMP), 171, 172 Epidermal growth factor (EGF), 324 Glycosylation ESI-MS. See Electrospray ionisation mass spectrometry k-casein, 152–153 post-translational modifications, 404 (ESI-MS) GMP. See Glycomacropeptide (GMP) Estemmosuchus, 5 GSHPOx. See Glutathione peroxidase (GSHPOx) Ethanol precipitation, 48 Gut-associated lymphoid tissue (GALT), 279 EWL. See Egg-white lysozyme (EWL) F H FABP. See Fatty acid-binding proteins (FABP) Hadrocodium wui, 2 Fatty acid-binding proteins (FABP), 495–496 Haptodus, 8 FBPs. See Folate-binding proteins (FBPs) HARP. See Heparin affin regulatory peptide (HARP) Feedback inhibitor of lactation (FIL), 326 HCV. See Hepatitis C virus (HCV) FIL. See Feedback inhibitor of lactation (FIL) Heat stability, 49 Fluorescence resonance energy transfer (FRET), 234 Heparin affin regulatory peptide (HARP), 320 Folate-binding proteins (FBPs), 324 Hepatitis C virus (HCV), 303 Fourier transform infrared (FTIR) Higher order structures b-casein, 169 molecular modeling k-casein, 172 as1-casein, 165–168 sodium caseinate, 177–179 as2-casein, 173–174 Fractionation b-casein, 168–170 and heterogeneity of caseins, 50–53 k-casein, 170–173 whey proteins, 57–58 mixed associations, 174–175 FRET. See Fluorescence resonance energy transfer (FRET) sodium caseinate, 176–179 FTIR. See Fourier transform infrared (FTIR) protein structure, 162–165 G three-dimensional molecular models, 163 b4-Galactosyltransferase-1 (b4Gal-T1), 23–26 HML. See Human milk lysozyme (HML) Gastrointestinal tract Hooded seal, 10 HT-29. See Human enterocyte-like cell line (HT-29) EGF and TGFa, 324 Human enterocyte-like cell line (HT-29), 304 IGF-1 and IGF-2, 323–324 Human milk lysozyme (HML), 365–367 Gel filtration Hylonomus, 6 casein preparation, 48 column chromatography, quantitation, 101–102 I Genetic polymorphism, 55 Ichthyophis glutinosus, 4 casein genes IEF. See Isoelectric focusing (IEF) IGF. See Insulin-like growth factor (IGF) vs. milk production traits, 497–498 IGF-binding proteins (IGFBPs), 323–324 population and phylogeny studies, 498–500 Immune function dairy ruminants bovine milk proteins, 468–475 b2-microglobulin, 321 caprine milk proteins, 474–484 lactoperoxidase, 322–323 ovine milk proteins, 484–490 lysozyme, 323 detection methods osteopontin, 321–322 DNA level, 465–466 proteose peptone 3, 322 mass spectrometry analysis, 464–465 TGFb1 and 2, 323 “top-down” process, 464–465 Immunoblotting, 116 human nutrition Immunochemical methods, quantitation bioactive peptides, 500–502 antibody arrays, 117 milk allergy, 502 applications, 117–123 milk-fat globule membrane proteins biosensor, 116–117 ABCG2, 495 ELISA, 115–116 butyrophilin, 493–494 general characteristics of, 114 FABP3, 495–496 immunoblotting, 116 fatty acid synthase, 493

Index 543 microparticle-enhanced nephelometric superoxide dismutase, 345–346 immunoassay, 116 xanthine oxidoreductase precipitation in gel, 116 assay methods, 343 significance and developments, 123 atherosclerosis, 344 Immunoglobulins (Igs) bactericidal activity, 344 biological fluids, 277 effect of processing, 343 classes and structure, 275–277 evolution of mammals, 344–345 mammary gland immunity heat treatment, 343–344 isolation of, 342 heterologous transfer, 286 lipid oxidation, 344 homologous transfer, 285–286 milk fat globules, 344 mammary gland transport nitrate reduction, 344 IgA and IgM, 280–281 Infrared spectroscopy, 91–98 IgG, 280 MIR, 92–95 neonate NIR, 95–98 colostrum, 283–285 secondary and tertiary structures, 110–111 and immunity, 283 Insulin-like growth factor (IGF), 323–324 milk immunoglobulins, 283–285 Intrinsically unstructured protein (IUP), passive immunity transfer intestinal uptake, 282 163, 164 neonate, 281–282 Ion exchange, column chromatography, 102–104 properties of, 277–279 Isoelectric focusing (IEF), 100–101 sources, 279 Isoelectric precipitation, 46–47 transport control, 281 IUP. See Intrinsically unstructured protein (IUP) whey proteins, 62–63 Indigenous enzymes K acid phosphatase Kjeldahl method assay methods, 360 isolation and characterisation, 360 analysis, 90–91 significance, 361 principle, 90 aldolase, 369 alkaline phosphatase L assay methods, 356–357 LAB. See Lactic acid bacteria (LAB) isolation and characterisation, 355–356 Lactadherin, 415–417 reactivation of, 357–358 a-Lactalbumin (a-La) significance, 358–359 amylase, 367–368 apoptotic effects, tumor, 269–270 b-N-acetylglucosaminidase, 368–369 lactose synthase catalase, 341–342 g-glutamyl transferase, 347–348 organization and regulation, 262–263 glutathione peroxidase, 347 role, 261–262 lactoperoxidase, 339–341 vs. Lysozyme lipases Ca-binding sites, 263, 264 bile salts-stimulated lipase, 351 phylogenetic tree, 265 esterases, 351–352 three-dimensional structures LPL, 349–351 b4-GT-I, 268–269 phospholipase, 351 binding, 268 lysozyme, 364–367 calcium-binding site, 266–268 minor enzymes, 339 catalytic domain, 267 nucleases Ca/Zn complex, 266 catalytic antibodies, oligonuclease activity, irregular b-turns, 265, 266 whey proteins, 60–62 363–364 Lactation 5’-nucleotidase, 364 amniotes ribonuclease, 361–363 amniotic egg, 5 proteinases Hylonomus, 6 cathepsin D, 353 Paleothyris, 6 human milk, 354 amphibian skin glands, 4 plasmin, 352–353 caecilians, 5 significance of, 354 Crocidura russula, 2 somatic cells, 354 Hadrocodium wui, 2 sulphydryl oxidase, 346 hooded seal milk, 10

544 Index Lactation (cont.) R↔S, 231 sauropsids, 5 unfolding–refolding, 231, 232 synapsids denaturation, 232–233 diphyodonty, 9 distribution, 214–216 eggs of, 5–6 evolutionary origin of, 27–31 Estemmosuchus, 5 evolutionary relationship, 241 incubating eggs, 9 function, 240–242 proto-lacteal glands, 7 genetic variants and primary structure, 217–221 sequential radiations, 7–9 immunochemical methods, quantitation, 117–118 terrestrial vertebrates, 2–3 isolation, 216–217 tetrapods ovine milk proteins, 490 proto-lacteal glands, 7 solution studies skin secretion, 2, 4 molecular properties, 228 terrestrial eggs, parental care of, 4–5 molecular size, 227–229 solubility, 227 Lactic acid bacteria (LAB), 46 structure, 221–225 Lactoferrin, 321 whey proteins, 58–60 Lactoperoxidase (LPO), 322–323, 339–341 biochemical properties Lipoprotein lipase (LPL), 349–351 concentrations and species differences, 296 Listeria monocytogenes, 301 historical perspective, 295 LPL. See Lipoprotein lipase (LPL) metal-and anion-binding properties, 296–297 LTF. See Lactoferrin (LTF) molecular weight and glycosylation, 296 Lysinoalanine (LAL), 528 resistant to proteolytic degradation, 297–298 Lysozyme, 410 tertiary structure, 296, 297 Lysozyme (Lz) Ca-binding sites, 263, 264 biological functions phylogenetic tree, 265 anti-adipogenic effects, 305 anticancer effects, 302–303 M antiviral effects, 303 MALDI-MS. See Matrix-assisted laser bacteriostasis/bactericidal effects, 301–302 bone homeostasis, 304–305 desorption/ionisation mass as growth factor, 304 spectrometry (MALDI-MS) immune function, 299–301 Mammary glands iron absorption, 305–307 apocrine glands, 10–12 multi-functionality, 299, 300 APSU and MPSU, 11–12 wound healing, 305 BMP signaling pathways, 12 Darwin’s theory of evolution, 1, 10 implications and significance of, 308–309 granular glands, 13 molecular biology, 298–299 immunity receptors heterologous transfer, 286 homologous transfer, 285–286 characteristics of, 308 innate immune system, 12–13 monocyte/macrophage system, 308 in mid-nineteenth century, 1 in small intestine, 307–308 opossums, 11 Lactoferrin (LTF), 410–411 oxytocin and mesotocin, 13 a-Lactoglobulin sweat glands, 10 bovine milk proteins, 474, 475 Mammary secretions, immunoglobulins caprine milk proteins, 484 biological fluids, 277 ovine milk proteins, 490 classes and structure, 275–277 b-Lactoglobulin (b-Lg) neonate amino acid environments, 225–227 colostrum and milk immunoglobulins, 283–285 binding studies and immunity, 283 EF loop, 238 origins of fatty acids, 234 IgA and IgM, 280–281 FRET study, 234 IgG, 280 ligand-binding parameters, 235–237 sources of, 279 macromolecule binding, 239–240 transport control, 281 pH, 234 passive immunity transfer, 281–282 biosynthesis and secretion, 213–214 properties of, 277–279 bovine milk proteins, 472–474 caprine milk proteins, 484 conformation and folding N↔R, 230–231 Q↔N, 229–230

Index 545 Mammo-pilo-sebaceous unit (MPSU), 11–12 MUC-15, 413 Mass spectrometry (MS) non-mucin proteins electrospray ionisation, 106–107 adipophilin, 418 MALDI, 106 butyrophilin, 413–415 milk proteins, molecular mass determination, lactadherin, 415–417 Milk fat globules (MFG) 107–108 adipophilin, 21 peptides, 109–110 apical blebs, 21–22 protein sequencing, 108–109 apocrine secretory mechanisms, 21–22 Matrix-assisted laser desorption/ionisation mass butyrophilin, 19–20 triacylglycerols, 19 spectrometry (MALDI-MS), 106 xanthine oxidoreductase, 20–21 Membrane filtration, 47–48 Milk protein concentrates (MPCs), 47 MFE. See Molybo-flavoenzyme (MFE) Milk proteins MFG. See Milk fat globules (MFG) casein-encoding genes MFGM proteins. See Milk fat globule membranes gene cluster, 432–433 individual gene structures, 433–434 (MFGM) proteins casein micelle MG. See Molten globule (MG) characteristics of, 68 b2-Microglobulin, 321 stability, 69–70 Milk structure, 70–74 casein protein preparation composition of, 43, 44 caseinates preparation, 49 features, 43 centrifugation after calcium enrichment, 47 lactose synthesis, 23–27 cryoprecipitation, 48 physiological functions, 43 ethanol precipitation, 48 production, 43 gel filtration, 48 acidification, 199–202 isoelectric precipitation, 46–47 cooling, 198–199 membrane filtration, 47–48 heating, 203–204 rennet coagulation, 48 Milk allergy, 502 salting-out methods, 47 Milk and products ultracentrifugation, 47 amino acid composition chromatin, 440–441 cis-regulatory elements, 436–438 bovine, 524 classical fractions of, 45 branched-chain amino acids, 522, 523 evolution, 34–35 casein, 522 gel electrophoresis applications, 53–54 indispensible amino acids protein content, 521 genetic polymorphism (see Genetic polymorphism) methionine and cysteine, 523 heterogeneity and fractionation, 50–53 sulphur-containing amino acids, 523 hormonal regulation, 436–438 whey protein, 522 interspecies comparison, 74–75 cheesemaking, 530–531 b-lactoglobulin (see b-Lactoglobulin (BLG)) digestibility vand utilisation, 524–526 mammary epithelial amino acid transport heat treatments Na+ dependent transport mechanisms, D-amino acids, 529 furosine accumulation, 529 448–449 lysinoalanine, 528, 529 Na+ independent transport mechanisms, Maillard reaction, 527 pasteurisation, 527 449–450 protein modifications, 529 peptides, 451 thermal denaturation, 527 transport and metabolism, 450 UHT treatment, 527 volume-activated amino acid transport, 450 homogenisation, 531 mammary secretory epithelium Milk fat globule membranes (MFGM) proteins biosynthetic-secretory pathway, 442 genetic polymorphism co-and post-translational modifications, 442–443 ABCG2, 495 Golgi apparatus, 445–446 butyrophilin, 493–494 hormonal regulation, 447 FABP3, 495–496 intracellular transport, 442–443 fatty acid synthase, 493 morphological organization, 442 MFGE8, 494–495 trans-Golgi network, 446–447 MUC-1, 491, 493 translocation, endoplasmic reticulum, protein-encoding gene, 496 glycosylation, 418–419 444–445 mucins MUC-1, 412–413

546 Index Milk proteins (cont.) MS. See Mass spectrometry (MS) MFGM (see Milk fat globule membranes (MFGM) MUC15. See Bovine mucin 15 (MUC15) proteins) Mucin 1 (MUC1), 327–328 microheterogeneity of caseins, 54–56 Mucins molecular properties of, 65–68 mRNAs, 441 MUC-1, 412–413 nomenclature of, 56 MUC-15, 413 nutritional quality (see Nutrition) Mucous secreting cells, 12 prolactin signal transduction, 439–440 Multiple anomalous dispersions (MAD), 112 quantitation of (see Quantitation) research, 44 N tissue specificity and developmental regulation, b-N-Acetylglucosaminidase (NAGase), 368–369 436 Native electrophoresis, quantitation, 99 transcriptional control, 438–439 Natively unfolded (NU), 163, 164 whey protein encoding genes NCN. See Non-casein nitrogen (NCN) a-lactalbumin gene and pseudogenes, 434 Neonatal Fc receptor (FcRn), 280 b-lactoglobulin-encoding gene and pseudogenes, Nitric oxide synthase (NOS) activity, 318 434 Nitrogen fractions, quantitation, 89 whey acidic protein, 435 NMR. See Nuclear magnetic resonance (NMR) whey proteins (see also Whey proteins) Non-casein nitrogen (NCN), 91 characteristics of, 58–65 Non-mucin proteins comparison with casein proteins, 49–50 fractionation of, 57–58 adipophilin, 418 preparation, 49, 56–57 butyrophilin, 413–415 lactadherin, 415–417 Milk teeth, 9 Non-protein nitrogen (NPN), 64–65, 91 Minor proteins NOS activity. See Nitric oxide synthase (NOS) activity Nuclear magnetic resonance (NMR) binding proteins milk proteins application, 114 FBPs, 324 principle, 112–113 riboflavin, 325 Nucleases, indigenous enzymes vitamin B12, 325 catalytic antibodies, oligonuclease activity, vitamin D, 324–325 363–364 BSA, 328 5’-nucleotidase, 364 gastrointestinal tract ribonuclease, 361–363 Nutrition EGF and TGFa, 324 bioactive peptides, 500–502 IGF-1 and IGF-2, 323–324 dietary proteins immune function b2-microglobulin, 321 amino acid requirements, 517–518 lactoperoxidase, 322–323 protein digestibility, 519–520 lysozyme, 323 protein requirements, 516–517 osteopontin, 321–322 protein utilisation, 520–521 proteose peptone 3, 322 milk allergy, 502 TGFb1 and 2, 323 milk and milk products mammary gland and maternal physiological amino acid composition, 521–524 cheesemaking, 530–531 regulatory function digestibility and utilisation, 524–526 FIL, 326 heat treatments, 526–529 leptin, 325–326 homogenisation, 531 PTHrP, 326–327 physiological activities, 531–533 relaxin, 327 mucins and glycoproteins, 327–328 O vascular system Origin of Species, 1 ACE, 319–320 Opossums, 11 angiogenins, 318–319 Osteopontin, 321–322 HARP, 320 Ovine milk proteins kininogen, 321 Molten globule (MG), 162–164, 269 as1-casein, 484, 486–487 Molybo-flavoenzyme (MFE), 20 as2-casein, 487, 489–490 Morganucodon, 8 b-casein, 487 MPCs. See Milk protein concentrates (MPCs) MPSU. See Mammo-pilo-sebaceous unit (MPSU)

Index 547 k-casein, 490 SDS electrophoresis, 99–100 a-lactalbumin, 490 secondary and tertiary structures, 110–114 b-lactoglobulin, 490 two-dimensional electrophoresis, 101 infrared methods, 91–98 P Kjeldahl method Paleothyris, 6 analysis, 90–91 Parathyroid hormone-related protein (PTHrP), 326–327 principle, 90 Parental care, 4–5 PAs. See Plasminogen activators (PAs) R Phospholipase, 351 RCM. See Reduced carboxymethylated (RCM) pIgR. See Polymeric immunoglobulin receptor (pIgR) Reduced carboxymethylated (RCM), 173, 174 Plasmin, 55–56, 119, 352–353 Relaxin, 327 Plasminogen activators (PAs), 352 Rennet coagulation, 48 PLG. See Plasminogen (PLG) Respiratory syncytial virus (RSV), 303 Polymeric immunoglobulin receptor (pIgR), 281 Riboflavin, 325 Polyproline II conformation (PPII), 163 Ribonucleases (RNase), 361–363 PPII. See Polyproline II conformation (PPII) RSV. See Respiratory syncytial virus (RSV) Plasminogen (PLG), 119 Pre-molten globule (PMG), 163, 164 S Proteinases, indigenous enzymes SAA. See Sulfur-containing amino acids (SAA) Salting-out methods, 47 cathepsin D, 353 Sauropsids, 5 human milk, 354 Secondary structures, quantitation plasmin, 352–353 significance of, 354 circular dichroism spectroscopy, 111–112 somatic cells, 354 infrared spectroscopy, 110–111 Proteolysis, 120 nuclear magnetic resonance, 112–114 Proteose peptone (PP) 3, 63–64, 322 X-ray crystallography, 112 Proto-lacteal glands, 7 Secretory calcium-binding phosphoproteins (SCPP), 14–18 Pseudomonas aeruginosa, 302 Sodium caseinate Pseudomonas fluorescens, 119–120 3D models, 176–179 PTHrP. See Parathyroid hormone-related protein FTIR studies, 177–179 laboratory preparations, 176 (PTHrP) Soy proteins, 123 Staphylococcus epidermis, 301 Q Sub-micelle model, 71–73 Quantitation Sulfur-containing amino acids (SAA), 27 Sulphydryl (SH) groups, 358 definition and analytical performance Sulphydryl oxidase (SHOx), 346 conversion factors, 89–90 Superoxide dismutase (SOD), 345–346 nitrogen fractions, 89 Supramolecule, casein acidification of milk, 199–202 immunochemical methods calcium sequestration, 202–203 antibody arrays, 117 cooling of milk, 198–199 applications, 117–123 EDTA, 202, 203 biosensor, 116–117 ethanol, 204–205 ELISA, 115–116 heating of milk, 203–204 general characteristics of, 114 interlocked lattice, 196–198 immunoblotting, 116 Sweat glands, 10 microparticle-enhanced nephelometric Synapsids immunoassay, 116 eggs of, 5–6 precipitation in gel, 116 Estemmosuchus, 5 significance and developments, 123 sequential radiations, 7–9 individual proteins T capillary electrophoresis, 101 Tensegrity hypothesis, higher order structures, 179–182 column chromatography, 101–105 (see also Tertiary structures Column chromatography) isoelectric focusing, 100–101 mass spectrometry, 105–110 microfluidic “lab-on-a-chip” techniques, 101 native electrophoresis, 99

548 Index lactoferrin, 296, 297 407–408 quantitation Whey protein concentrates (WPCs), 47–48 Whey protein isolates (WPIs), 48 circular dichroism spectroscopy, 111–112 Whey proteins infrared spectroscopy, 110–111 nuclear magnetic resonance, 112–114 characteristics of X-ray crystallography, 112 blood serum albumin, 62 Tetrapods immunoglobulins, 62–63 proto-lacteal glands, 7 a-lactalbumin, 60–62 terrestrial eggs, parental care of, 4–5 b-lactoglobulin, 58–60 Thrinaxodon, 8 nonprotein nitrogen, 64–65 TOCSY. See Total correlation spectroscopy (TOCSY) proteose peptones, 63–64 Total correlation spectroscopy (TOCSY), 113 whey acidic protein, 60 Transforming growth factor (TGF)b1, 323 Transmission electron microscopy (TEM), 187–188, comparison with caseins amino acid composition, 49–50 192, 194, 198 biosynthesis site, 50 Two-dimensional electrophoresis, 101 heat stability, 49 physical state, 50 U solubility at pH 4.6, 49 Ultracentrifugation, 47 fractionation of, 57–58 V immunochemical methods, quantitation, 117 Variable number of tandem repeats (VNTR), 418 preparation, 49, 56–57 Vascular system WPCs. See Whey protein ACE, 319–320 concentrates (WPCs) angiogenins, 318–319 HARP, 320 X kininogen, 321 Xanthine oxidoreductase (XOR), 20–21 Vitamin B12-binding protein, 325 Vitamin D-binding protein, 324–325 assay methods, 343 Vitellogenins, 18 atherosclerosis, 344 VNTR. See Variable number of tandem repeats bactericidal activity, 344 effect of processing, 343 (VNTR) evolution of mammals, 344–345 heat treatment, 343–344 W isolation of, 342 WAP. See Whey acidic protein (WAP) lipid oxidation, 344 Whey acidic protein (WAP), 31–34, 60, milk fat globules, 344 nitrate reduction, 344 X-ray crystallography, 112