No alpha-lactalbumin-like activity detected in a low molecular mass protein fraction of rat epididymal extract

1993 ◽  
Vol 5 (2) ◽  
pp. 229 ◽  
Author(s):  
Y Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Protein Fraction ◽  
Bovine Milk ◽  
Specific Effect ◽  
Radioactive Product ◽  
Ion Exchange Column ◽  
Synthesis Activity ◽  
Enzyme Source ◽  
High Voltage Electrophoresis ◽  
Alpha Lactalbumin

The same low M(r) protein fraction of epididymal luminal fluid as that studied previously by Hamilton in 1981 was assayed for alpha-lactalbumin (alpha-lac) activity with bovine milk galactosyltransferase (GalTase) as the enzyme source and bovine serum albumin (BSA) to make the total protein concentrations of all the samples in each assay constant. No alpha-lac activity could be detected in this fraction. When glucose was used as an acceptor, radioactivity passing through the ion exchange column used to retain the remaining UDP-galactose did increase with the amount of the proteins of the low M(r) fraction, but this increase was observed not only for samples with an acceptor but also for samples without. The increased radioactive product co-migrated in high-voltage electrophoresis with galactose, not lactose. When GlcNAc was used as an acceptor, the situation was the same, and the increased radioactive product co-migrated with galactose, not LacNAc. No inhibition of bovine milk GalTase activity by the low M(r) proteins was observed. Addition of protein, either BSA or the low M(r) fraction of epididymal luminal fluid, to assay medium that contained no proteins other than GalTase enhanced the GalTase activity both in forming lactose in the presence of glucose and also LacNAc in the presence of GlcNAc. It appears that the earlier reports of alpha-lac-like activity in epididymal fluids and extracts may have been due to the presence of enzymes liberating free galactose from UDP-galactose and/or a stimulatory non-specific effect of the protein in the solutions on the lactose synthesis activity of the GalTase.

.alpha.-Lactalbumin enhances the gelation properties of bovine serum albumin

1993 ◽  
Vol 41 (7) ◽  
pp. 1053-1057 ◽  
Author(s):  
Naotoshi. Matsudomi ◽  
Toru. Oshita ◽  
Kunihiko. Kobayashi ◽  
John E. Kinsella
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Alpha Lactalbumin

Influence of Amitrole Upon Protein Metabolism in Bean Plants

Weed Science ◽  
1968 ◽  
Vol 16 (2) ◽  
pp. 222-226 ◽  
Author(s):  
John C. Brown ◽  
Mason C. Carter
Keyword(s):  
Free Radical ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radical Formation ◽  
Bean Plants ◽  
Free Radical Formation ◽  
Synthesis Activity ◽  
Hydrolysis Of ◽  
Bean Protein

No effect was shown of 3-amino-l,2,4-triazole (amitrole) upon the incorporation of alanine or histidine into soluble protein in bean (Phaseolus vulgaris L.) hypocotyls grown in darkness. The metabolic derivative of amitrole, β-(3-amino-1,2,4-triazolyl-l-)α-ala-nine (hereinafter referred to as 3-ATAL), also had no effect upon histidine incorporation. Serine incorporation was increased 56% in the presence of amitrole, but this may result from a reduction of endogenous serine pools. No evidence indicates a general disruption of protein synthesis. Activity from amitrole-5-14C was readily incorporated into bean protein, but hydrolysis revealed no 3-ATAL. Most of the activity was recovered as amitrole. Amitrole in the presence of riboflavin and light attacked bovine serum albumin, probably by free radical formation. Hydrolysis of bovine serum albumin revealed mainly amitrole. Apparently, the entry of amitrole into bean protein is by free radical formation.

ANTI-BOVINE SERUM ALBUMIN AND ANTI-ALPHA LACTALBUMIN IN THE SERUM OF CHILDREN AND ADULTS

PEDIATRICS ◽  
1965 ◽  
Vol 35 (4) ◽  
pp. 571-588
Author(s):  
Richard M. Rothberg ◽  
Richard S. Farr
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gamma Globulin ◽  
Age Distribution ◽  
Skin Tests ◽  
Positive Skin ◽  
Antigen Antibody ◽  
Alpha Lactalbumin

1. Because precipitin, hemagglutination, and complement-fixation tests measure secondary manifestations of antigen-antibody interactions and are sometimes negative even after a primary antigen-antibody reaction has occurred in vitro, the incidence and amount of anti-bovine serum albumin (BSA) was evaluated in the sera from 900 children and adults by means of precipitating I131-labeled BSA-antibody complexes with 50% saturated ammonium sulfate. A similar study using I131-labeled alpha lactalbumin (ALA) was performed on 718 of this same group of sera. 2. Antibody to BSA was detected more frequently among children (75%) than among young adults 16 to 40 years of age (25%), or among older age groups (8%). 3. The incidence of detectable antibody to ALA had the same age distribution, but only half the frequency as anti-BSA. 4. In contrast to the near absence of antibody in the cord serum as measured by hemagglutination titers using red cells coated with milk proteins, most of the antibody detected in maternal sera in the present study was able to cross the placental barrier and was present in the cord sera. 5. The incidence of both anti-BSA or anti-ALA was the same in males and females. 6. If a given sera bound both IBSA and IALA, the anti-BSA activity was usually, but not always, greater than the anti-ALA activity. 7. No shared antigenicity was detected between IBSA and ovalbumin, insulin, protamine, diptheria, and tetanus toxoid, pertussis vaccine, poliomyelitis vaccine, and influenza vaccine. The apparent inhibiting effects of unlabeled bovine gamma-globulin and ALA on IBSA binding were probably due to trace amounts of BSA in these protein preparations. 8. BSA, ovalbumin, and bovine gamma-globulin had no detectable shared anti-genicity with IALA. 9. Positive skin tests to milk or BSA did not correlate with the anti-BSA levels measured in the serum. 10. The incidence of persons with anti-BSA and anti-ALA was comparable among the "patient" and "well" populations. Ten of the 31 sera with the greatest capacity to bind IBSA were from the "well" population, the remaining 21 sera were from children with a variety of disease states.

scholarly journals Reassembly of the peptidyltransferase centre of larger subparticles of rabbit reticulocyte ribosomes from a core-particle and split-protein fraction

1976 ◽  
Vol 160 (3) ◽  
pp. 533-546 ◽  
Author(s):  
R A Cox ◽  
P Greenwell
Keyword(s):  
Protein Fraction ◽  
Protein Fractions ◽  
Molar Ratio ◽  
Core Particle ◽  
Original Activity ◽  
Two Dimensional Gel Electrophoresis ◽  
The Core ◽  
Split Protein ◽  
Synthesis Activity ◽  
Protein Moiety

We report the reconstruction, from a core-particle and split-protein fraction, of the larger subribosomal particle of rabbit reticulocytes. The reassembled particle was active in polyphenylalanine synthesis and in the puromycin reaction. The core-particles and split-protein fractions were obtained by treatment of the larger subparticle with salt solutions containing NH4+ and Mg2+ in the molar ratio 40:1 over the range 2.25-2.75 M-NH4Cl/56-69mM-MgCl2 at 0° C. This treatment led to the loss of about eight proteins (approx. 17% of the protein moiety), which were found wholly or largely in the split-protein fraction as shown by two-dimensional gel electrophoresis. The core particle retained 5S rRNA and had much decreased (no more than 10% of control) ability to function in the puromycin reaction or in poly (U)-directed polyphenylalanine synthesis. Activity was recovered when the recombined core-particle and split-protein fractions were dialysed overnight at 4° C against 0.3M-NH4Cl/15mM-MgCl2/1mM-dithiothreitol/15% (v/v) glycerol/20mM-Tris/HCl, pH 7.6, and then heated for 1 h at 37° C. The recovery was 40-80% of the original activity. Raising the concentration of MgCL2 to 300 mM in 2.5 M-NH4CL led to the removal of seven rather than eight proteins, and the core particle remained active in the puromycin reaction. We infer that the protein retained by raising the concentration of Mg2+ is an essential component of the peptidyltransferase centre of the ribosome.

Purification and Identification of Lactoferrin from Bovine Milk

2012 ◽  
Vol 524-527 ◽  
pp. 2290-2293
Author(s):  
Ying Ying Kong ◽  
Meng Liu ◽  
Wei Di ◽  
Cong Wang ◽  
Ming Du ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Membrane Filtration ◽  
Bovine Milk ◽  
Gel Filtration ◽  
Exchange Column ◽  
Sds Page ◽  
Ion Exchange Column

Lactoferrin has many kinds of bioactivities which have attracted more and more attention. In the present study, lactoferrin from bovine milk was isolated and purified by membrane filtration, series of chromatography on SP Sepharose Big Bead ion exchange column and Superdex 200 gel filtration column. The purified lactoferrin was identified by SDS-PAGE compared with the lactoferrin standard.

scholarly journals Alpha-Lactalbumin Enriched Whey Protein Concentrate to Improve Gut, Immunity and Brain Development in Preterm Pigs

Nutrients ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 245
Author(s):  
Charlotte Holme Nielsen ◽  
Yan Hui ◽  
Duc Ninh Nguyen ◽  
Agnethe May Ahnfeldt ◽  
Douglas G. Burrin ◽  
...  
Keyword(s):  
Human Milk ◽  
Whey Protein ◽  
Bovine Milk ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Microbial Metabolites ◽  
Neonatal Development ◽  
Organ Weights ◽  
Gut Immunity ◽  
Alpha Lactalbumin

Human milk is rich in nutritional factors, such as alpha-lactalbumin (α-Lac), and important for neonatal development, but nutrient supplementation may be required for optimal growth. Using a pig model, we hypothesized that α-Lac-enriched whey protein concentrate (WPC) supplementation improves neonatal development. Cesarean-delivered preterm pigs were fed either dilute bovine milk (REF) or REF milk supplemented with WPC with normal (STANDARD-ALPHA) or high (HIGH-ALPHA) α-Lac. Clinical, gut, immune and cognitive endpoints (open field, T-maze) were assessed and tissues collected at Day 19. The growth of STANDARD-ALPHA and HIGH-ALPHA were higher than REF (31 vs. 19 g/kg/d). Most organ weights, gut, immunity and brain variables were similar between WPC groups. HIGH-ALPHA had a higher bone mineral content, colon microbial diversity and an abundance of specific bacteria and microbial metabolites, and tended to show a faster food transit time (p = 0.07). Relative to REF, WPC pigs showed higher relative organ weights, blood amino acids, blood neutrophil function, and microbial metabolites, but lower brush-border enzyme activities and plasma cortisol. Cognition outcomes did not differ among the groups. In conclusion, WPC supplementation of milk improved some growth, gut and immunity parameters in preterm pigs. However, increasing the α-Lac content beyond human milk levels had limited effects on the immature gut and developing brain.

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