scholarly journals Studies on Parturient Paresis in Dairy Cows. V. On the Composition and Calcium Binding Capacity of Two Bovine Serum Protein Fractions, with Special Regard to Parturient Paresis

1970 ◽  
Vol 11 (1) ◽  
pp. 89-102
Author(s):  
Gunnar Carlström
Keyword(s):  
Dairy Cows ◽  
Serum Protein ◽  
Calcium Binding ◽  
Bovine Serum ◽  
Binding Capacity ◽  
Protein Fractions ◽  
Special Regard ◽  
Parturient Paresis ◽  
Bovine Serum Protein

Evaluation of usefulness of a commercial agarose gel electrophoresis kit (QuickGel SP) for bovine serum protein electrophoresis

2017 ◽  
Vol 20 (3) ◽  
pp. 527-534
Author(s):  
Y. Okatsu ◽  
N. Yamagishi ◽  
K. Hatate ◽  
B. Devkota
Keyword(s):  
Serum Protein ◽  
Gel Electrophoresis ◽  
Bovine Serum ◽  
Protein Fractions ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Serum Samples ◽  
Cellulose Acetate Electrophoresis ◽  
Γ Globulins ◽  
Bovine Serum Protein

Abstract The aim of this study was to show the usefulness of a commercial agarose gel electrophoresis (AGE) kit (QuickGel SP) for separating bovine serum protein fractions in comparison with conventional cellulose acetate electrophoresis (CAE). Serum protein bands were verified using five reference reagents corresponding to albumin and α1-, β1-, β2-, and γ-globulins. AGE clearly revealed six separated fractions of albumin and α1-, α2-, β1-, β2-, and γ-globulin fractions in 100% and 77.8% in serum samples of dairy cows from the healthy (n=27) and diseased groups (n=27), respectively. The α1- and α2-globulins were not separated by CAE in 14.8% and 96.3% of the samples from the healthy and diseased groups, respectively, whereas β2- and γ-globulin were not separated by CAE in 96.3% and 100% of the samples from the healthy and diseased groups, respectively. More than 94% of the points for the α-globulin fractions (α1- and α2-globulins), the β-γ-globulin fractions (β1-, β2-, and γ-globulins), and the albumin/globulin ratio between AGE and CAE were within agreement on the Bland-Altman plots. However, the mean biases were not near zero in the albumin and β-γ-globulin fractions. These results suggest that the high-resolution commercial AGE kit can be utilized to separate bovine serum protein fractions.

Isolation of a calcium-binding peptide from bovine serum protein hydrolysates

2012 ◽  
Vol 21 (6) ◽  
pp. 1663-1667 ◽  
Author(s):  
Dong-Won Choi ◽  
Ji-Hye Lee ◽  
Ho-Hyun Chun ◽  
Kyung Bin Song
Keyword(s):  
Serum Protein ◽  
Calcium Binding ◽  
Bovine Serum ◽  
Protein Hydrolysates ◽  
Binding Peptide ◽  
Bovine Serum Protein

scholarly journals An on–off–on gold nanocluster-based fluorescent probe for sensitive detection of organophosphorus pesticides

RSC Advances ◽  
2017 ◽  
Vol 7 (87) ◽  
pp. 55199-55205 ◽  
Author(s):  
Q. J. Luo ◽  
Z. G. Li ◽  
J. H. Lai ◽  
F. Q. Li ◽  
P. Qiu ◽  
...  
Keyword(s):  
Fluorescent Probe ◽  
Serum Protein ◽  
Bovine Serum ◽  
Organophosphorus Pesticides ◽  
Gold Nanoclusters ◽  
Sensitive Detection ◽  
Gold Nanocluster ◽  
Highly Sensitive ◽  
Bovine Serum Protein

In this study, a highly sensitive fluorescent probe based on bovine serum protein-protected gold nanoclusters (BSA-AuNCs) was developed for the determination of organophosphorus pesticides (OPs).

Studying the fetal bovine serum protein corona associated with single and multilayer graphene oxide nanomaterials

2017 ◽  
Vol 280 ◽  
pp. S181
Author(s):  
Lidiane Silva Franqui ◽  
Antônio Carlos Borges ◽  
Marcelo Alexandre de Farias ◽  
Rodrigo Villares Portugal ◽  
Adriana Franco Paes Leme ◽  
...  
Keyword(s):  
Graphene Oxide ◽  
Serum Protein ◽  
Bovine Serum ◽  
Fetal Bovine Serum ◽  
Protein Corona ◽  
Multilayer Graphene ◽  
Fetal Bovine ◽  
Fetal Bovine Serum Protein ◽  
Bovine Serum Protein

Seasonal variations in serum protein fractions of dairy cows during different physiological phases

2011 ◽  
Vol 21 (6) ◽  
pp. 1439-1443 ◽  
Author(s):  
Giuseppe Piccione ◽  
Vanessa Messina ◽  
Daniela Alberghina ◽  
Claudia Giannetto ◽  
Stefania Casella ◽  
...  
Keyword(s):  
Dairy Cows ◽  
Serum Protein ◽  
Seasonal Variations ◽  
Protein Fractions

scholarly journals The Use of Bovine Serum Protein as an Oral Support Therapy Following Coronavirus Challenge in Calves

2002 ◽  
Vol 85 (5) ◽  
pp. 1249-1254 ◽  
Author(s):  
J.D. Arthington ◽  
C.A. Jaynes ◽  
H.D. Tyler ◽  
S. Kapil ◽  
J.D. Quigley
Keyword(s):  
Serum Protein ◽  
Bovine Serum ◽  
Bovine Serum Protein

scholarly journals Study on the Quality of Lyophilized Human Diploid Cell Rabies Vaccine Using Microcarrier Technology

2015 ◽  
Vol 4 (1) ◽  
pp. 4
Author(s):  
Yong Cai ◽  
Rong Zhou ◽  
Shengyou Li ◽  
Qiong Huang ◽  
Gangqiang Yang ◽  
...  
Keyword(s):  
Serum Protein ◽  
Bovine Serum ◽  
Diploid Cell ◽  
Rabies Vaccine ◽  
Antibiotic Residues ◽  
Human Diploid Cell ◽  
Residual Content ◽  
Human Diploid Cells ◽  
Safety And Stability ◽  
Bovine Serum Protein

<p>The aim is to study the potency, purity, safety, and stability of the lyophilized human diploid cell rabies vaccine (HDCV). The viruses were harvested from infected human diploid cells (MRC-5 strain) which were cultured in a microcarrier bioreactor. After harvest, purification, inactivation and lyophilization, HDCV was produced. The potency of vaccines was measured by NIH method; the bovine serum protein residual content and the antibiotic residues were tested by ELISA method; the endotoxin content was detected by semi quantitative gel method; the safety of vaccine was determined <em>in vivo</em>. Among 6 batches of HDCV, the lowest immunizing potency was 4.79 IU/ml, whilst the highest was 6.03 IU/ml; the lowest bovine serum protein residual content was 12.41 ng/dose, whilst the highest was 31.74 ng/Dose; the content of antibiotic residues was from 2.20 ng/ml to 4.00 ng/ml; endotoxin levels were all lower than 50 EU/dose. All the mice and guinea pigs vaccinated were all alive, and the body weight of each mouse also increased. The stability was investigated by determining the water content and potency of the vaccine placed in 37±1 °C for 4 weeks and 2-8 °C for 48 months, respectively. The results indicate all the quality index accords with the standards of “Pharmacopoeia of the People's Republic of China 2010, 3 Volumes”. HDCV shows satisfactory potency, purity, safety, and stability.</p>

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