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At least 793 records · Page 44Linked to original sources
PubMed1994

Bovine colostrum ultrafiltrate supplemented with adult bovine serum and transferrin: an effective FBS substitute for cultivation of Vero and CHO-K1 cells.

A mixture containing an ultrafiltrate fraction (UF) of bovine colostrum (6.7%), adult bovine serum (BS) (1%), and human holo-transferrin (hTF) (5 mg/liter) was developed for cultivation of Chinese hamster ovary cells (CHO-K1) and African green monkey kidney cells (Vero). The growth-supporting activity of the mixture (UF/BS/hTF) was comparable to that of 1 to 10% fetal bovine serum (FBS) and considerably better than 1 to 2% BS. Cells could be directly seeded from FBS-supplemented medium to UF/BS/hTF-supplemented medium without any weaning period, even at initial plating density of 1700 cells/ml. Vero and CHO-K1 cells were cultivated in UF/BS/hTF-supplemented media for up to 43 days without any apparent reduction in growth. The UF/BS/hTF mixture could also be used as a freezing medium. Cells were passaged twice in the mixture, frozen, and stored at liquid N2 for 11 wk. After thawing, the viability of Vero and CHO-K1 cells was reduced 13 and 7%, respectively, and both cell lines started to grow well. Additional hTF could be replaced with bovine holo-transferrin, although a high concentration (150 mg/liter) should be used for CHO-K1 cells. The results suggest that the UF/BS/hTF mixture provides a new economical alternative to FBS in cultivation of Vero and CHO-K1 cells in the presence of reduced protein amounts.

Animals↗
PubMed2003

Effect of bovine colostrum supplementation on the composition of resistance trained and untrained limbs in healthy young men.

This study examined the effect of bovine colostrum (BC) supplementation on the tissue composition of resistance trained (T) and untrained (UT) limbs. Using a double-blind design, subjects were randomly allocated to 60 g day(-1) of BC ( n=17) or whey protein (WP) ( n=17) during 8 weeks of resistance training of the elbow flexors (EF) of their non-dominant arm (T). Axial magnetic resonance images of both upper arms, maximal voluntary isometric torque (MVC) of EF, and the one repetition maximum (1RM) for bicep curls were measured pre- and post-supplementation. There were no differences in macronutrient intakes ( P>0.28) or the volume of training completed by T ( P=0.98) between the two groups. T of BC experienced a significantly greater increase in circumference [BC 2.3 (3.0)%, WP 0.0 (4.2)%; P=0.05] and cross-sectional area (CSA) [BC 4.2 (6.0)%, WP -0.2 (8.3)%; P=0.05] compared with WP, due principally to a greater increase in skin and subcutaneous fat (SSF) CSA [BC 5.5 (10.9)%, WP -2.7 (14.1)%; P=0.03]. No tissue compartment changed significantly in UT of either group ( P>0.05). MVC and 1RM increased for T and UT in both groups ( P<0.05), but the increases were not different between groups ( P>0.32). Since the SSF compartment increased in T but not UT, and fat turnover in adipocytes is under hormonal control and would not be localised to one arm, we suggest that the increase in SSF CSA in T of BC may have been due to an increase in skin CSA, rather than fat.

Adolescent↗
PubMed2003

Bovine colostrum supplementation does not affect plasma buffer capacity or haemoglobin content in elite female rowers.

It has been reported that bovine colostrum (BC) supplementation improves buffer capacity (beta) during exercise, but whether the improvement results from changes in tissue and/or blood buffer systems has not been determined. The purpose of the present study was to examine the effect of supplementation with BC on blood buffer systems. Thirteen elite females rowers were supplemented with 60 g.day(-1) of either BC ( n=6) or whey protein (WP, n=7) during 9 weeks of pre-competition training in a randomised, double-blind, placebo-controlled, parallel design. All subjects undertook the study as a group and completed the same training program. Resting haemoglobin (Hb) concentration and plasma buffer capacity (pbeta) (determined by titration with HCl) were measured pre- and post-supplementation. There were no differences in macronutrient intakes ( P>0.56) or training volumes ( P>0.99) between BC and WP during the study period. There were no differences in Hb [BC 13.28 (0.28) mg.dl(-1), WP 13.70 (0.26) mg.dl(-1); P=0.45] or pbeta [BC 14.8 (1.1) nmol HCl.ml(-1).pH(-1), WP 14.8 (0.5) nmol HCl.ml(-1).pH(-1); P=0.68] between groups at week 0. pbeta increased in both groups during the study period ( P<0.001), but the increases were not significantly different between groups ( P=0.52). Hb did not change significantly in either group ( P=0.35). These data indicate that supplementation with BC does not affect pbeta or Hb. We therefore suggest that adaptations in tissue buffer systems are responsible for the previously reported increases in buffer capacity that result from BC supplementation.

Adaptation, Physiological↗
PubMed2004

Colostrum from healthy Brazilian women inhibits adhesion and contains IgA antibodies reactive with Shiga toxin-producing Escherichia coli.

UNLABELLED: Although Shiga toxin-producing Escherichia coli (STEC) has been isolated in Brazil, severe manifestations of the infection, such as haemorrhagic colitis and haemolytic-uraemic syndrome, are extremely rare in our population. Enteropathogenic Escherichia coli (EPEC) is the main aetiological agent of acute infantile diarrhoea in Brazil. There are many similarities between STEC and EPEC, such as the ability to produce attaching and effacing (A/E) lesions and some virulence-associated factors. Our aim was to investigate the presence of anti-STEC antibodies in healthy people living in an EPEC endemic area. Colostrum samples collected from 51 women living in low socio-economic conditions were analysed. Two STEC strains: O111:H- (Stx1) and O157:H7 (Stx2), and one EPEC strain (O111:H-) were used in the bacterial adhesion assays to HEp-2 cells, in the Stx1 and Stx2 cytotoxicity assays on Vero cells, in immunoblotting and in ELISA assays. All the samples strongly inhibited the adhesion of the three strains and contained SIgA antibodies reactive with antigens of EPEC O111:H-, STEC O111:H- and STEC O157:H7, mainly STEC and EPEC 94 kDa adhesin intimin. High titres of anti-LPS O111 antibodies were found in many samples. Nevertheless, the cytotoxic effect of both Stx1 and Stx2 on Vero cells was not neutralised by any sample. CONCLUSION: Our results suggest that Brazilian people may be exposed to Shiga toxin-producing Escherichia colimore frequently than previously thought or alternatively there may be a cross reactive immunity between enteropathogenic Escherichia coliand Shiga toxin-producing Escherichia coli.

Adult↗
PubMed2005

Obtaining hyperimmune anti-Cryptosporidium parvum ovine colostrum. A study of the humoral immune response in immunized sheep.

Three ewes were immunized five times over a 2-month period prior to giving birth by intramuscular injection, oral administration and intramammary infusion of antigen and viable or freeze-dried Cryptosporidium parvum oocyst solution emulsified with Freund's complete and incomplete adjuvant. Two animals served as controls and another two as adjuvant controls. Serum was collected at first immunization and thereafter every 2 to 4 weeks. Colostrum and milk were collected as well. All samples were assayed for C. parvum-specific antibodies using an enzyme-linked immunosorbent assay methodology, and Western blotting was used to recognize the C. parvum antigens. Hyperimmunization resulted in a progressive and significant increase in specific anti-C. parvum serum IgG, IgA and IgM titres, with the highest values noted at the point of lambing. Titres decreased slightly in milk, although they were in all cases higher than those in the control animals. Moreover, some 30 bands of C. parvum were recognized.

Animals↗
PubMed2000

Experimental infection of colostrum deprived piglets with porcine circovirus 2 (PCV2) and porcine reproductive and respiratory syndrome virus (PRRSV) potentiates PCV2 replication.

Experimental infection of colostrum-deprived (CD) pigs with a combined inoculum of porcine circovirus 2 (PCV2) and porcine reproductive and respiratory syndrome virus (PRRSV) potentiated the replication and distribution of PCV2 virus, when compared with pigs inoculated with PCV2 alone. The replication and distribution of PRRSV in dually infected pigs was not enhanced, when compared to pigs inoculated with PRRSV alone. The mechanisms involved in the potentiation of PCV2 replication in PCV2/PRRSV and PCV2/porcine parvovirus (PPV) dually infected pigs may relate to the fact that monocyte/macrophage cell types are common targets of these 3 viruses.

Animals↗
PubMed1992

Purification, crystallization, and X-ray diffraction studies of lactotransferrin from buffalo colostrum.

Lactotransferrin is an iron-binding protein. It has been purified from buffalo colostrum. The purified lactotransferrin has been crystallized in 10% ethanol solution. The crystals are orthorhombic and the space group is P2(1)2(1)2(1) with unit cell dimensions a = 161.70 A, b = 155.75 A, c = 113.48 A. The asymmetric unit contains three molecules of the protein with a solvent content of about 59%. The crystals were stable in the X-ray beam and diffract beyond 3.5 A resolution. The native data have been collected and the structure determination is in progress.

Animals↗
PubMed1975

Trypsin inhibitor from cow colostrum. Isolation, electrophoretic characterization and immunologic properties.

Trypsin inhibitor from cow colostrum has been purified by affinity chromatography of colostral proteins on insolubilized trypsin. The method described compares favourably, in both simplicity and yield, with previous methods developed for the isolation of this inhibitor. Gel electrophoresis followed by characterization of antitrypsin activity allows the demonstration of four molecular forms of bovine colostral trypsin inhibitor in both crude colostral whey and purified preparations of the inhibitor. Immunoelectrophoresis of each of these materials with antisera specific for this inhibitor reveals a single precipitation line of broad anodic mobility. By immunodiffusion tests, the precipitation lines in preparations of purified inhibitor and colostral whey appear immunologically identical. In contrast, absence of crossed reactivity was observed between bovine colostral trypsin inhibitor and trypsin inhibitors of bovine serum. This strongly suggests the high specificity of this inhibitor as a colostral and milk constituent.

Animals↗
PubMed1987

Chemical structure of three neutral trisaccharides isolated in free form from bovine colostrum.

Three neutral trisaccharides, which comprise 25.1% of the neutral oligosaccharide other than lactose, were isolated from bovine colostrum, obtained 6 h after parturition, by l.c. on amino silica gel. The chemical structures were identified, by methylation analysis with direct m.s. and g.l.c.-m.s., and by structural analysis with 13C-n.m.r., as beta-D-Galp-(1----4)-[alpha-L-Fucp-(1----3)-]-D-GlcNAc (3-fucosyl-N-acetyllactosamine), beta-D-Galp-(1----3)-beta-D-Galp-(1----4)-D-Glc (3'-galactosyllactose), and beta-D-Galp-(1----6)-beta-D-Galp-(1----4)-D-Glc (6'-galactosyllactose). The The first-named compound was a novel oligosaccharide from mammalian milk.

Animals↗
PubMed1994

Studies of the neutral trisaccharides of goat (Capra hircus) colostrum and of the one- and two-dimensional 1H and 13C NMR spectra of 6'-N-acetylglucosaminyllactose.

Four neutral trisaccharides were isolated from goat colostrum by dialysis, and ion-exchange, activated charcoal column, preparative paper, and Bio-Gel P-4 column chromatography. The following structures were elucidated by GC analysis of hydrolysis products and by 400-MHz 1H NMR spectroscopy: alpha-L-Fuc p-(1-->2)-beta-D-Gal p-(1-->4)-D-Glc, alpha-D-Gal p- (1-->3)-beta-D-Gal p-(1-->4)-D-Glc, beta-D-Gal p-(1-->3)-beta-D-Gal p-(1-->4)-D-Glc, and beta-D-Gal p-(1-->6)-beta-D-Gal p-(1-->4)-D-Glc. beta-D-Glc pNAc-(1-->6)-beta-D-Gal p-(1-->4)-D-Glc, previously reported to be present in goat milk, was not detected in this study. beta-D-Glc pNAc-(1-->6)-beta-D-Gal p-(1-->4)-D-Glc (6'-N- acetylglucosaminyllactose) was prepared by beta-D-galactosidase digestion of beta-D-Gal p-(1-->3)[beta-D-Glc pNAc-(1-->6)]-beta-D-Gal p-(1-->4)-D-Glc (lacto-N-novotetraose) and characterized by one- and two-dimensional NMR spectroscopy at 600 MHz.

Animals↗
PubMed1984

Demonstration and partial purification of lactoperoxidase from human colostrum.

A peroxidase with stability, chromatographic and immunoreactive properties similar to that of bovine lactoperoxidase has been partly purified from human colostrum. Hydrophobic interaction chromatography on Phenyl-Sepharose C1-4B gave a 10-fold purification with an apparent recovery of about 45%. The enzyme was quantitatively and specifically adsorbed to beads of anti-lactoperoxidase (bovine)-Protein A-Sepharose. No adsorption of the enzyme was observed on immunoadsorbent columns prepared with high-titre polyclonal antibodies raised against human myeloperoxidase and human eosinophile peroxidase.

Chromatography, Affinity↗
PubMed1994

Bovine colostrum ultrafiltrate: an effective supplement for the culture of mouse-mouse hybridoma cells.

An ultrafiltrate fraction (UF) of bovine colostrum has been successfully used as a cell culture supplement for growth and monoclonal IgG antibody production of cultured mouse-mouse hybridomas derived from spleen cells. In this study we compared the ability of UF to support growth and antibody production of IgA hybridomas derived from Peyer's patch cells with that of an IgG hybridoma cell line. One IgG (LPC2) and two IgA hybridoma cell lines (RB3 and P2E7) were used as models. The optimal UF concentration for Ig production and cell growth for both the IgA hybridoma RB3 and the IgG hybridomas was 5-10%. Initial plating density was found to be a critical factor for IgA hybridoma cell growth: the IgA hybridomas required a seeding density of at least 70,000 cells/ml to grow compared to 15,000 IgG hybridoma cells/ml (Pakkanen et al., 1992). The addition of small amounts (up to 2%) of FBS in 10% UF supplemented medium did not enhance IgA production or cell growth. RB3 and LPC2 cells seeded at equal density and grown in 10% UF for 8 days attained maximum cell densities at 3-4 days that were 58% (RB3) or 34% (LPC2) lower than those in 10% FBS, but the total amounts of monoclonal antibody produced were 73% and 83%, respectively, of that in 10% FBS. Thus, Ig production per cell was 22-27% higher in 10% UF than in 10% FBS. Hybridoma cells could be cultured for at least 5 weeks without any reduction in growth rates, if medium was partially but not completely replaced twice a week. This suggests that hybridoma cells maintained in UF supplemented medium secrete growth promoting factors. Cells maintained in UF for up to 5 weeks sustained similar monoclonal antibody production rates as in short term culture. These results show that UF can be used as an economical and effective hybridoma culture supplement for the production of both IgG and IgA antibodies.

Animals↗
PubMed1983

Immunologically active nonapeptide fragment of a proline-rich polypeptide from ovine colostrum: amino acid sequence and immunoregulatory properties.

It has been previously found that a proline-rich polypeptide (PRP) isolated from ovine colostrum has a regulatory effect on the immune response. To study the relationship between the structure of PRP and its immunomodulatory properties, the polypeptide was digested by chymotrypsin. Products of the proteolysis were separated by gel filtration and three fractions were obtained: PRP-1, PRP-2 and PRP-3. The activity of the fractions was compared with the activity of the untreated PRP. It was found that PRP-1 was inactive, whereas PRP-2 and PRP-3 showed an activity in the regulation of the immune response assayed by measurement of PFC, and by studying effects on delayed hypersensitivity, formation of autologous rosette-forming cell, and sensitivity of thymocytes to hydrocortisone. The activity of PRP-2 and PRP-3 was comparable to the activity of PRP. The PRP-3 fraction of low mol. wt was further purified and a pure nonapeptide of mol. wt 1000 (PRP-3b) was isolated. The amino acid sequence of PRP-3b was: Val--Glu--Ser--Tyr--Val--Pro--Leu--Phe--Pro. The nonapeptide showed the full spectrum of biological activities of PRP. Comparison of terminal amino acid suggested that PRP-3b was neither the NH2- nor the COOH-terminal fragment of PRP. The amino acid sequence of the nonapeptide indicated that PRP-3b is different from other known immunomodulators.

Amino Acid Sequence↗
PubMed1987

Immunoregulatory properties of synthetic peptides, fragments of a proline-rich polypeptide (PRP) from ovine colostrum.

It has been previously found that a proline-rich polypeptide (PRP) isolated from ovine colostrum has a regulatory effect on the immune response. A nonapeptide fragment Val-Glu-Ser-Tyr-Val-Pro-Leu-Phe-Pro was isolated from the chymotryptic digest of PRP. The nonapeptide showed biological activity similar to PRP. The determined amino acid sequence was now confirmed by synthesis. Synthetic nonapeptide as well as its C-terminal hexapeptide, Tyr-Val-Pro-Leu-Phe-Pro, showed biological activity similar to PRP and the nonapeptide obtained from PRP.

Animals↗
PubMed1993

Purification and characterization of IgG1 and IgG2 from buffalo (Bubalus bubalis) serum and colostrum.

Buffalo IgG1 and IgG2 were purified from serum and colostrum using salt precipitation, dialysis, gel filtration and ion-exchange chromatography. Their purity was monitored by immunodiffusion and immunoelectrophoresis using anti-heavy chain specific sera and SDS-PAGE. Selective binding of IgG2 to protein-A was used to remove IgG2 from IgG1 preparations. The IgG1 and IgG2 had a molecular mass (Mr) of 162.0 and 161.5 kD, respectively and were found to consist of heavy (H) and light (L) chains. The H and L chains had Mr of 58 and 24 kD, respectively. Reduction-alkylation followed by gel filtration was used for the isolation of H and L chains. While intact H chains were obtained, the L chains appeared to be cleaved into 14 kD molecules and smaller fragments. The mean hexoses content of the serum IgG1 and IgG2 was 1.81 +/- 0.02% and 0.70 +/- 0.02%, respectively. The corresponding values for colostral IgG1 and IgG2 were 1.76 +/- 0.01% and 0.78 +/- 0.08%. Both the IgG subclasses activated homologous complement. These results suggest that buffalo and cattle IgG subclasses have many common characteristics and minor differences.

Animals↗
PubMed1996

Purification of bovine beta 2-microglobulin from colostrum and its complete amino acid sequence.

Bovine beta 2-microglobulin (beta 2-m) was purified from colostrum milk in two chromatographic steps: anion-exchange chromatography, and gel filtration. The amino acid sequence was determined to confirm that the purified protein was beta 2-m. A molecular weight of 11.8 kDa beta 2-m was estimated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Bovine beta 2-m consists of 98 amino acid residues and contains one disulfide linkage connecting residues 25 and 79. The amino acid sequence determined by this study is different from a previously published sequence at three sites, but agrees with the amino acid sequence from cDNA. Thus, we can conclude that the amino acid sequence determined in this study is correct.

Amino Acid Sequence↗