scholarly journals Characterization of Pregnancy Specific Protein B (PSPB) from Placenta Foetalis (Cotyledon) Friesian Holstein Cows

2008 ◽  
Vol 2 (1) ◽  
Author(s):  
Abdul Samik
Keyword(s):  
Western Blot ◽  
Optical Density ◽  
Early Pregnancy ◽  
Molecular Size ◽  
Specific Protein ◽  
Holstein Cows ◽  
Sds Page ◽  
Immunohistochemical Techniques ◽  
Protein B

This research was aimed to find out a substance that was useful in early pregnancy diagnosis of Friesian Holstein cows. Pregnancy Specific Protein B (PSPB) was isolated, purified and partially characterized from cotyledon Friesian Holstein cows. Characterization of PSPB protein was conducted using SDS-PAGE and Western Blot. Antisera were developed against PSPB and by immunohistochemical techniques the protein was localized to the binucleated cells of the cotyledon. The estimated molecular size of Friesian Holstein cows PSPB was 59.88 kDa with the concentration of PSPB protein in cotyledon was 6480 ng/ml. PSPB protein could induce anti-PSPB antibody with the value of optical density (OD) were 0.179±0.0102 (before immunization); 1.466±0.3288 (3rd week after immunization); 1.936±0.4754 (1st week after booster;) and 2.256±0.4842 (2nd week after booster).

scholarly journals Production and characterization of monoclonal antibodies to the edta extract of Leptospira interrogans, serovar icterohaemorrhagiae

1996 ◽  
Vol 29 (5) ◽  
pp. 483-489
Author(s):  
Lilian Terezinha de Queiroz Leite ◽  
Mauricio Resende ◽  
Wanderley de Souza ◽  
Elizabeth R.S. Camargos ◽  
Matilde Cota Koury
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Western Blot ◽  
Silver Staining ◽  
Colloidal Gold ◽  
Leptospira Interrogans ◽  
Outer Envelope ◽  
Lethal Challenge ◽  
Sds Page

Monoclonal antibodies (MABs) ivere produced against an etbylenediaminetetraacetate (EDTA) extract of Leptospira interrogans serovar icterohaemorrhagiae being characterized by gel precipitation as IgM and IgG (IgGl and IgG2b). The EDTA extract was detected as several bands by silver staining in SDS-PAGE. In the Western blot the bands around 20 KDa reacted with a monoclonal antibody, 47B4D6, and was oxidized by periodate and was not digested by pronase, suggesting that the determinant is of carbohydrate nature, lmmunocytochemistry, using colloidal gold labeling, showed that an EDTA extract determinant recognized by monoclonal antibody 47B4D6, is localized under the outer envelope of serovar icterohaemorrhagiae. Hoe AIAB raised against the EDTA extract was not able to protect hamsters from lethal challenge with virulent homologous leptospires.

scholarly journals Characterization of Inhibin from Culture and Non Culture of Granulose Cells for Monoclonal Antibody of Inhibin Production

2010 ◽  
Vol 4 (1) ◽  
Author(s):  
Amiruddin Amiruddin ◽  
Tongku Nizwan Siregar ◽  
Amalia Sutriana ◽  
Dwinna Aliza ◽  
T. Armansyah
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Western Blot ◽  
Total Amino Acid ◽  
Multiple Ovulation ◽  
Sds Page ◽  
Isoelectric Points ◽  
Granulose Cells

This study has long-term objectives to obtain immunogenic prototype that can be used to induce multiple ovulation in goats. Working steps of this study were begun with the collection of ovarium from goats, collection of granulose cells, culture of granulose and characterization of molecular weight and isoelectric point (pI) of inhibin protein of granulose cells obtained from culture and non-culture of granulose cells, and followed by preparation of monoclonal antibody toward inhibin. The results showed that inhibin isolated either from culture or non-culture of granulose cells produced a 32 kDa band. Molecular weight of inhibin was measured by Western Blot. The 32 kDa band of SDS PAGE product appeared on Western Blot result was inhibin molecules produced by granulose cells collected fom culture and non-culture of granulose cells that can be identified by Mab-inhibin. Product of IEF gel electrophoresis suggested that inhibin molecule collected from culture of granulose cells has no charge at isoelectric points ranging from 5-6, depends on its total amino acid composition.

Partial characterization of the immunosuppressive properties of pregnancy-specific protein B (PSPB)

1990 ◽  
Vol 33 (1) ◽  
pp. 220 ◽  
Author(s):  
M.M. Dunbar ◽  
T.S. Wong ◽  
C.A. Ruder-Montgomery ◽  
B.P. Chew ◽  
R.G. Sasser
Keyword(s):  
Specific Protein ◽  
Partial Characterization ◽  
Protein B

scholarly journals Pregnancy-specific protein B, progesterone concentrations and embryonic mortality during early pregnancy in dairy cows

Reproduction ◽  
1988 ◽  
Vol 83 (1) ◽  
pp. 215-223 ◽  
Author(s):  
P. Humblot ◽  
S. Camous ◽  
J. Martal ◽  
J. Charlery ◽  
N. Jeanguyot ◽  
...  
Keyword(s):  
Dairy Cows ◽  
Early Pregnancy ◽  
Specific Protein ◽  
Embryonic Mortality ◽  
Protein B

scholarly journals Pregnancy-Specific Protein B Induces Release of an Alpha Chemokine in Bovine Endometrium

Endocrinology ◽  
1999 ◽  
Vol 140 (1) ◽  
pp. 542-545 ◽  
Author(s):  
Kathy J. Austin ◽  
Cathy P. King ◽  
Judith E. Vierk ◽  
R. Garth Sasser ◽  
Thomas R. Hansen
Keyword(s):  
Affinity Chromatography ◽  
Primary Culture ◽  
Early Pregnancy ◽  
Specific Protein ◽  
Molar Ratio ◽  
Interferon Tau ◽  
Western Blots ◽  
Chemotactic Protein ◽  
Uterine Proteins ◽  
Protein B

Abstract Pregnancy-specific protein B (PSPB), is secreted from binucleate trophoblast of the bovine conceptus as early as day 15 of pregnancy. The objective of this experiment was to determine if PSPB induced uterine proteins. PSPB was purified from day 120 cotyledons using antibody-based affinity chromatography. Endometrium from day 14 non-pregnant cows (n = 3) was prepared for explant (3H-Leu added) culture. Radiolabeled proteins released into medium were dialyzed, separated using 1D-PAGE, and detected using fluorography and densitometry. PSPB (0, 0.5, 5, 25 & 50 nM) caused a concentration-dependent increase in the release of a radiolabeled 8-kDa uterine protein. Western blots revealed that the 8-kDa protein cross-reacted with antibody against granulocyte chemotactic protein-2 (GCP-2). PSPB also induced release of GCP-2 by bovine endometrial (BEND) cells in primary culture. The induction of GCP-2 by PSPB was blocked by addition of antiserum against PSPB (1:4 molar ratio). This is the first indication that PSPB has a hormonal role in inducing GCP-2, an alpha chemokine that also is induced by interferon-tau during early pregnancy. This chemotactic cytokine may be integral to mediating adhesion, inflammation and angiogenesis associated with early implantation.

Expression, Purification and Characterization of Amantadine Receptor in Escherichia coli

2012 ◽  
Vol 161 ◽  
pp. 88-93 ◽  
Author(s):  
Hai Xin Sun ◽  
Li Min Cao ◽  
Hong Lin ◽  
Fang Lv
Keyword(s):  
Inclusion Bodies ◽  
Equilibrium Dialysis ◽  
Molecular Size ◽  
M2 Protein ◽  
Purification And Characterization ◽  
E Coli ◽  
His Tag ◽  
Sds Page ◽  
Fast Flow

In order to obtain large quantities of broadly selective receptor as one diagnose agent to detect amantadine residue, the M2 protein gene with a His-tag was ligated into pET11a and transferred into E. coli BL21 (DE3) cell. The recombinant E. coli was cultured in liquid LB culture. SDS-PAGE result showed the recombinant M2 protein (rM2) was expressed as insoluble inclusion bodies with about 18KDa in molecular size. rM2 protein was further recognized by Western blot and purified by Ni Sepharose 6 Fast Flow and then refolded. The equilibrium dialysis result showed the rM2 protein had the binding constant of 1.1×105, and stoichiometry of 4.2. The above result showed the rM2 has the potential as biological diagnose agent to the detection of amantadine residue.

scholarly journals Isolation, Purification, and Characterization of Pregnancy-Specific Protein B from Elk and Moose Placenta1

1999 ◽  
Vol 61 (4) ◽  
pp. 1056-1061 ◽  
Author(s):  
Fan Huang ◽  
Diane C. Cockrell ◽  
Thomas R. Stephenson ◽  
James H. Noyes ◽  
R. Garth Sasser
Keyword(s):  
Specific Protein ◽  
Purification And Characterization ◽  
Protein B
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