scholarly journals Neonatal role of milk folate-binding protein: studies on the course of digestion of goat's milk folate binder in the 6-d-old kid

1983 ◽  
Vol 50 (3) ◽  
pp. 589-596 ◽  
Author(s):  
D. N. Salter ◽  
A. Mowlem
Keyword(s):  
Molecular Weight ◽  
Folic Acid ◽  
Binding Capacity ◽  
Stomach Contents ◽  
Soluble Form ◽  
Folate Binding Protein ◽  
Total Recovery ◽  
Goat’S Milk ◽  
Goat's Milk

1. Groups of kids were reared from birth to 5 d on goat's milk. On the 6th day five of the kids received by bottle a morning feed of goat's milk with [3H]folic acid added to saturate the folate-binding proteins (FBP) (Expt 1); three kids received raw goat's milk containing only the endogenous folate and hence a large surplus folate-binding capacity (FBC) (Expt 2). The contents of the stomach, duodenum, jejunum and ileum were recovered by washing out 1·5 h after feeding (Expt 1) or at 0·5, 1 and 3·5 h after feeding (Expt 2).2. Recovery of [3H]folic acid 1·5 h after feeding (Expt 1) in all segments was 58·4%, mainly in a soluble form, most of this being in the stomach (37·0%) and ileum (14·3%). No surplus FBC was found in any gut segment. Sephadex G-75 chromatography of the soluble fractions of the contents of the various gut segments showed that [3H]folic acid remained bound to FBP throughout the stomach and small intestine. The bound [3H]folic acid exhibited a molecular weight of 81000 in stomach contents, similar to that in the milk feed, presumably representing an aggregated form of the FBP, whereas in the intestinal contents its molecular weight was 39000 indicating dissociation to monomer due to dilution in the recovery process.3. In Expt 2, the total recovery of free FBP in all four gut segments was 67, 54 and 23% respectively at 0·5, 1 and 3·5 h after the milk feed, and the distribution of FBP along the gut at 1 h was similar to that of [3H]folic acid-labelled FBP at 1·5 h in Expt 1. In mature goat's milk the endogenous 5-methyltetrahydrofolate was shown to be associated with species of molecular weight 80000 and 38000.4. The results indicate that goat's-milk FBP is relatively resistant to digestionby gastric and intestinal enzymes in vivo in the kid and survives along the length of thesmall intestine.5. The implications of the findings are discussed in relation to the possible influence of FBP on uptake of folate by mucosal cells and their relevance to neonatal folate nutrition.

scholarly journals The Influence of Trace-Mineralized Salt upon the Vitamin B12 and Folic Acid Content of Goat's Milk

1953 ◽  
Vol 36 (1) ◽  
pp. 29-32 ◽  
Author(s):  
R.A. Collins ◽  
R.E. Boldt ◽  
C.A. Elvehjem ◽  
E.B. Hart
Keyword(s):  
Folic Acid ◽  
Vitamin B12 ◽  
Acid Content ◽  
Goat’S Milk ◽  
Goat's Milk

scholarly journals Influence of goat's-milk folate-binding protein on transport of 5-methyltetrahydrofolate in neonatal-goat small intestinal brush-border-membrane vesicles

1988 ◽  
Vol 59 (3) ◽  
pp. 497-507 ◽  
Author(s):  
Dallynn. Salter ◽  
Peter Blakeborough
Keyword(s):  
Brush Border ◽  
Brush Border Membrane ◽  
Binding Protein ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Molar Ratio ◽  
Folate Binding Protein ◽  
Intestinal Brush Border ◽  
Goat’S Milk ◽  
Goat's Milk

1. The influence of goat's-milk folate-binding protein (FBP) on the uptake of 5-methyltetrahydrofolate (MTHF) by brush-border-membrane vesicles prepared from the small intestine of the 6-d-old goat was investigated using a rapid-filtration assay.2. Uptake of MTHF by the membrane vesicles was strongly enhanced by FBP within the pH range 4·5-6·5, with an optimum at pH 5-5·5.3. Both the initial rate of MTHF uptake and uptake of MTHF at equilibrium were markedly increased in the presence of FBP.4. Uptake of MTHF by brush-border-membrane vesicles was maximal when the molar ratio FBP: MTHF was 1·0-2·5.5. The relation between pH and 125I-labelled FBP binding to the membranes was similar to that for uptake of MTHF, with an optimum at pH 5.6. In experiments in which the osmotic pressure of the incubation medium was progressively increased with cellobiose, 125I-labelled FBP was found to be taken up primarily by binding to the brush-border-membrane surface.7. Uptake of 125I-labelled FBP was time-dependent and saturable, with a Km of 0·39 (SE 0·07) μM and Vmax of 6·73 (SE 0·92) μg/mg protein.8. Experiments in which various milk proteins (cow FBP, goat FBP, α-lactalbumin, β-lactoglobulin, bovine serum albumin and lactoferrin) were allowed to compete in turn with 125I-labelled FBP for uptake by brush-border-membrane vesicles indicated that high-affinity binding was probably specific to FBP, although lactoferrin reduced uptake possibly by non-specific coating of the mucosal surface.9. It was concluded that a folate transport mechanism mediated by the FBP in milk exists at the intestinal brush border of neonatal goats. It is suggested that this may reinforce the developing endogenous transport system.

scholarly journals Digestion of the zinc in human milk, cow's milk and a commercial babyfood: some implications for human infant nutrition

1986 ◽  
Vol 55 (2) ◽  
pp. 209-217 ◽  
Author(s):  
Peter Blakeborough ◽  
Michael I. Gurr ◽  
Dallyn N. Salter
Keyword(s):  
Molecular Weight ◽  
Human Milk ◽  
High Molecular Weight ◽  
Stomach Contents ◽  
Human Infant ◽  
Soluble Form ◽  
Cow’S Milk ◽  
Low Molecular Weight ◽  
Cow's Milk ◽  
Molecular Weight Form

1. The digestion of zinc present in human milk, cow's milk and a commercial babyfood was compared, using the piglet as a model for the human infant.2. In piglets given human milk the pH of stomach contents was approximately 1 and 0.4 units lower than that of animals given respectively cow's milk and babyfood. The pH values of intestinal contents were approximately neutral and did not vary with the type of feed.3. Hard casein curds were present throughout the stomachs and small intestines of animals fed on cow's milk or babyfood and between 55 and 70% Zn in these digesta samples were recovered in an insoluble form by centrifugation. In contrast, little solid material was observed in the digesta of animals fed on human milk, and 57 and 93% respectively of the Zn in digesta were recovered in a soluble form in the stomach and small intestine.4. Soluble fractions prepared by centrifugation of digesta were analysed by filtration on Sephadex G-150. After any of the three feeds, soluble Zn in stomach contents was mainly in a low-molecular-weight form. In intestinal samples, however, Zn was present in low- and high-molecular-weight forms. Whilst there were similar amounts of Zn in the low-molecular-weight form in all samples, approximately three times as much of the total intestinal Zn was in a soluble high-molecular-weight form complexed to proteins in the animals fed on human milk compared with those fed on cow's milk or babyfood.5. Analysis of protein-bound soluble Zn in intestinal samples on SDS-polyacrylamide gels resulted in a similar pattern of proteins for all feeds. Results indicated that at least some of these proteins were derived from intestinal secretions of the piglet.6. Some implications of these results in respect of the mode of digestion of Zn and its biological availability to the human infant are discussed.

The folic acid activity of some milk foods for babies

1968 ◽  
Vol 35 (1) ◽  
pp. 85-90 ◽  
Author(s):  
J. E. Ford ◽  
K. J. Scott
Keyword(s):  
Folic Acid ◽  
Breast Milk ◽  
Human Milk ◽  
Folic Acid Supplementation ◽  
Cow’S Milk ◽  
Acid Supplementation ◽  
Cow's Milk ◽  
Goat’S Milk ◽  
Liquid Milk ◽  
Goat's Milk

SummaryFolic acid activity was determined for National Dried Milk and for 5 proprietary dried milk foods for babies, for a proprietary liquid milk baby food and for 8 brands of tinned evaporated milk. For comparison, values were determined for mature breast milk, for raw bulk cow's milk, for bottled pasteurized cow's milk and for goat's milk.Human milk and raw and pasteurized cow's milk all had much the same folate activity, equivalent to about 54 µg folic acid/1. Values for goat's milk were much lower, around 6 µg/1.Values for the reconstituted baby milks ranged from 9 to 65 µg/1, though only 2 of the products had markedly lower values than breast milk. The question is discussed whether the folic acid requirement in infants can be met by formulas based on cow's milk without having recourse to folic acid supplementation.

scholarly journals The heterogeneity and properties of folate binding proteins from chronic myelogenous leukemia cells

Blood ◽  
1975 ◽  
Vol 46 (6) ◽  
pp. 855-867 ◽  
Author(s):  
CD Fischer ◽  
M da Costa ◽  
SP Rothenberg
Keyword(s):  
Molecular Weight ◽  
Folic Acid ◽  
Chronic Myelogenous Leukemia ◽  
Binding Proteins ◽  
Binding Protein ◽  
Myelogenous Leukemia ◽  
Leukemia Cells ◽  
Folate Binding Protein ◽  
Binding Factor ◽  
Chronic Myelogenous Leukemia Cells

Previous studies have demonstrated that some chronic myelogenous leukemia cells contain a macromolecular binding factor for folic acid. This binder, which previously was believed to be a single factor, has now been resolved into two distinct binding proteins. Separation of each binder was obtained by DEAE chromatography of the partially purified lysate of chronic myelogenous leukemia cells. One binder has a molecular weight of 30;000–35,000, and the second binder has a molecular weight of 40,000-45,000. Both proteins bind the mono-, di-, and triglutamates of folic acid, N10-methyl-folate, dihydro-folate, and N5-methyltetrahydrofolate. Neither binder has determinants for N5- formyltetrahydrofolate or methotrexate. The preferred substrates for both binders appear to be the fully oxidized and partially reduced folates rather than the fully reduced folates. The lower-molecular- weight folate binding protein shows reversible binding with partially and fully reduced folates but irreversible binding with oxidized folates. This property suggests that this binder may have some function in the transport and storage of folate. The higher-molecular-weight folate binding protein, however, has only slight reversibility of binding with the partially and fully reduced folates, and it is therefore more difficult to postulate a physiologic function for this binding factor.

scholarly journals The heterogeneity and properties of folate binding proteins from chronic myelogenous leukemia cells

Blood ◽  
1975 ◽  
Vol 46 (6) ◽  
pp. 855-867 ◽  
Author(s):  
CD Fischer ◽  
M da Costa ◽  
SP Rothenberg
Keyword(s):  
Molecular Weight ◽  
Folic Acid ◽  
Chronic Myelogenous Leukemia ◽  
Binding Proteins ◽  
Binding Protein ◽  
Myelogenous Leukemia ◽  
Leukemia Cells ◽  
Folate Binding Protein ◽  
Binding Factor ◽  
Chronic Myelogenous Leukemia Cells

Abstract Previous studies have demonstrated that some chronic myelogenous leukemia cells contain a macromolecular binding factor for folic acid. This binder, which previously was believed to be a single factor, has now been resolved into two distinct binding proteins. Separation of each binder was obtained by DEAE chromatography of the partially purified lysate of chronic myelogenous leukemia cells. One binder has a molecular weight of 30;000–35,000, and the second binder has a molecular weight of 40,000-45,000. Both proteins bind the mono-, di-, and triglutamates of folic acid, N10-methyl-folate, dihydro-folate, and N5-methyltetrahydrofolate. Neither binder has determinants for N5- formyltetrahydrofolate or methotrexate. The preferred substrates for both binders appear to be the fully oxidized and partially reduced folates rather than the fully reduced folates. The lower-molecular- weight folate binding protein shows reversible binding with partially and fully reduced folates but irreversible binding with oxidized folates. This property suggests that this binder may have some function in the transport and storage of folate. The higher-molecular-weight folate binding protein, however, has only slight reversibility of binding with the partially and fully reduced folates, and it is therefore more difficult to postulate a physiologic function for this binding factor.

scholarly journals Reduction of energy demand during ultrafiltration of goat’s milk

2020 ◽  
Vol 207 ◽  
pp. 01016
Author(s):  
Mariya Dushkova ◽  
Siyka Kodinova
Keyword(s):  
Molecular Weight ◽  
Flow Rate ◽  
Energy Demand ◽  
Reduction Ratio ◽  
Volume Reduction ◽  
Feed Flow Rate ◽  
Working Pressure ◽  
Goat’S Milk ◽  
Low Levels ◽  
Goat's Milk

This experimental investigation aimed to establish the energy demand depending on the working pressure (0,2 MPa and 0,5 MPa), the feed flow rate (190 dm3/h and 330 dm3/h) and the volume reduction ratio (2 and 4) during ultrafiltration of goat’s milk by membrane with molecular weight cut-off 10 kDa. The energy demand increased with the rise of all three factors investigated. The most significant effect had the pressure followed by the volume reduction ratio and the feed flow rate. The lowest value of energy demand (12,29 kWh/m3) was obtained at low levels of all factors (pressure of 0,2 MPa, feed flow rate of 190 dm3/h, volume reduction ratio of 2).

scholarly journals Fermented Goat Milk Supplementation in Rats Hypercholesterolmic on Malonyldialdehyde and Description of Liver Histopathology

2017 ◽  
Vol 8 (1) ◽  
pp. 1
Author(s):  
Chanif Mahdi ◽  
Untari H. ◽  
Padaga Padaga
Keyword(s):  
Therapeutic Effect ◽  
Bioactive Peptides ◽  
Dose Range ◽  
Goat Milk ◽  
Fermented Milk ◽  
Milk Product ◽  
Goat’S Milk ◽  
Protease Enzyme ◽  
Goat's Milk

Empirically, fermented milk product has been proven to improve and cure for several certain diseases. Bioactive peptides were produced through a fermentation process in goat milk promotes many benefits on body health. The present study revealed that goat milk was fermented using starter commercial 3% to produced yoghurt increased protein content significantly. By using SDS- PAGE, showed that the decomposition of protein fraction was better than the fresh goat milk. Results then were analyzed by LC-MS/MS and found out that there were three kinds of bioactive each peptide consisted of 16 amino acids and were protected from the action of the protease enzyme. Goat's milk yoghurt was treated per oral in mice after hypercholesterolemic diet for 14 days with dose range of 300 mg/kg; 600 mg/kg; and 900 mg/kg for 4 weeks (28 days). The results demonstrated three type of bioactive peptides performed activity as anti-hypercholesterolemia on mice models which showed highly significant (P <0.01) on the production of malondialdehyde (MDA) compared to control. Furthermore, goat milk yogurt also reduced MDA level and decreased fats accumulation in mice. Goat's milk yoghurt at dose of 600 mg/kg was able to provide the best therapeutic effect in lowering MDA level and with dose of 900 mg/kg also gave the best therapeutic effect in reducing the fat accumulation on liver. Based on histopathology observation, it was revealed that fermented goat milk reduced cells damage in liver. In summarize, these findings suggest that fermented goat milk promotes another activities as anti-hypercholesterolemia based on in vivo study.Keywords: Fremented goat milk, hypercholeterolmia, malonyldialdehyde, liver hispathology

Scanning Tunneling Microscopy and Atomic Force Microscopy of Enzymes and Enzyme Complexes

1990 ◽  
Vol 48 (3) ◽  
pp. 174-175
Author(s):  
Ronald D. Edstrom ◽  
Xiuru Yang ◽  
Mary E. Gurnack ◽  
Marcia A. Miller ◽  
Rui Yang ◽  
...  
Keyword(s):  
Cell Biology ◽  
Inorganic Ions ◽  
Bulk Liquid ◽  
Soluble Form ◽  
Scanning Tunneling ◽  
Tunneling Microscopy ◽  
Metabolic Channeling ◽  
Simplistic Notion ◽  
Soluble Enzymes

Many of the questions in biochemistry and cell biology are concerned with the relationships of proteins and other macromolecules in complex arrays which are responsible for carrying out metabolic sequences. The simplistic notion that the enzymes we isolate in soluble form from the cytoplasm were also soluble in vivo is being replaced by the concept that these enzymes occur in organized systems within the cell. In this newer view, the cytoplasm is organized and the “soluble enzymes” are in fact fixed in the cellular space and the only soluble components of the cell are small metabolites, inorganic ions etc. Further support for the concept of metabolic organization is provided by the evidence of metabolic channeling. It has been shown that for some metabolic pathways, the intermediates are not in free diffusion equilibrium with the bulk liquid in the cell but are passed along, more or less directly, from one enzyme to the next.

In Vitro and in Vivo Comparison of Binding of 99m-Tc-Iabeled Anti-CEA MAb F33-104 with 99m-Tc-labeled Anti-CEA MAb BW431/26

1999 ◽  
Vol 38 (04) ◽  
pp. 115-119
Author(s):  
N. Oriuchi ◽  
S. Sugiyama ◽  
M. Kuroki ◽  
Y. Matsuoka ◽  
S. Tanada ◽  
...  
Keyword(s):  
Nude Mice ◽  
Binding Capacity ◽  
Colon Adenocarcinoma ◽  
Human Colon ◽  
Cell Binding ◽  
Vitro Binding ◽  
Labeling Method ◽  
Human Colon Adenocarcinoma

Summary Aim: The purpose of this study was to assess the potential for radioimmunodetection (RAID) of murine anti-carcinoembryonic antigen (CEA) monoclonal antibody (MAb) F33-104 labeled with technetium-99m (99m-Tc) by a reduction-mediated labeling method. Methods: The binding capacity of 99m-Tc-labeled anti-CEA MAb F33-104 with CEA by means of in vitro procedures such as immunoradiometric assay and cell binding assay and the biodistribution of 99m-Tc-labeled anti-CEA MAb F33-104 in normal nude mice and nude mice bearing human colon adenocarcinoma LS180 tumor were investigated and compared with 99m-Tc-labeled anti-CEA MAb BW431/26. Results: The in vitro binding rate of 99m-Tc-labeled anti-CEA MAb F33-104 with CEA in solution and attached to the cell membrane was significantly higher than 99m-Tclabeled anti-CEA MAb BW431/261 (31.4 ± 0.95% vs. 11.9 ± 0.55% at 100 ng/mL of soluble CEA, 83.5 ± 2.84% vs. 54.0 ± 2.54% at 107 of LS 180 cells). In vivo, accumulation of 99m-Tc-labeled anti-CEA MAb F33-104 was higher at 18 h postinjection than 99m-Tc-labeled anti-CEA MAb BW431/26 (20.1 ± 3.50% ID/g vs. 14.4 ± 3.30% ID/g). 99m-Tcactivity in the kidneys of nude mice bearing tumor was higher at 18 h postinjection than at 3 h (12.8 ± 2.10% ID/g vs. 8.01 ± 2.40% ID/g of 99m-Tc-labeled anti-CEA MAb F33-104, 10.7 ± 1.70% ID/g vs. 8.10 ± 1.75% ID/g of 99m-Tc-labeled anti-CEA MAb BW431/26). Conclusion: 99m-Tc-labeled anti-CEA MAb F33-104 is a potential novel agent for RAID of recurrent colorectal cancer.

Sign in / Sign up

Export Citation Format

Share Document