6 research outputs found
ISOLATION, PARTIAL PURIFICATION AND IMMUNOBIOCHEMICAL CHARACTERIZATION OF INHIBIN FROM GOAT OVARIAN FOLLICULAR FLUID
In the present study Inhibin was purified from goat ovarian follicular fluid by Gel filtration chromatography on Sephacryl S-200. SDS PAGE of purified inhibin revealed the molecular weight of 55 kDa. The purified follicular fluid had been found to be immunoreactive by DID test and Western Blot analysis when treated against hyperimmune sera
PURIFICATION AND BIOCHEMICAL CHARACTERIZATION OF IgG FROM SERUM OF YAK ( BOS GRUNNIENS )
In the present study Immunoglobulin G was purified from serum of Yak by gel filtration chromatography on Sephacryl S-200. SDS- PAGE of purified yak IgG showed four major polypeptides of 62.94 kDa, 53.29 kDa 29.22 and 28.21 kDa. The purified Immunoglobulin has been found to be immuno-reactive by DID test and Western Blot analysis when treated against hyper-immune sera
EMERGENCE OF COAGULASE POSITIVE METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS ISOLATED FROM BUFFALO MASTITIS MILK SAMPLES
The present study was undertaken to screen methicillin resistant Staphylococcus aureus (MRSA) in mastitis
buffalo milk samples from northern India. A total of 120 buffalo mastitis milk samples were collected from individual
quarter over a one year period mainly from animals reared by marginal farmers. The isolates were presumptively confirmed
by growing the organism in selective media and biochemical tests. A total of 52 samples were presumptively confirmed as
Staphylococci on the basis of growth in Mannitol Salt Agar (MSA); out of which 12 samples were coagulase positive
Staphylococcus aureus (S. aureus) by growth in Baird Parker Agar (BPA) and tube coagulase test. Antibacterial profiling
and growth on Methicillin resistant Staphylococcus aureus (MeReSa) Agar indicated five isolates as MRSA. Further PCR
of specific gene segments and their subsequent characterization based on 16S ribosomal RNA, of staphylo-coagulase and
mecA confirmed the findings. The study accentuates the importance of determining the causal agents of mastitis,
antibacterial profiling so as to enable the clinicians and researchers to intervene and adopt effective control measures
PARTIAL PURIFICATION AND IMMUNO-BIOCHEMICAL CHARACTERISATION OF FERTILITY ASSOCIATED PROTEIN OF KARAN FRIES BULL SEMINAL PLASMA
The objective of the present study was detection, isolation, partial purification and
immunobiochemical characterization of fertility associated protein in the seminal plasma of high
prolific Karan fries bull. Seminal plasma of Karan Fries bull was partially purified by gel filtration
chromatography and analyzed by 10% SDS-PAGE for their polypeptide profile. PAGE analysis
revealed major band of 55 kDa, and 26 kDa. Hyperimmune serum was raised in rabbit against crude
seminal plasma protein. Single precipitin line was observed in DID test when each of the partially
purified 26 kDa and 55 kDa proteins were reacted with hyperimmune serum. These proteins were
also found to be immunoreactive against hyperimmune serum in Western blot technique
Plasma mineral profiles and hormonal activities of normal cycling and repeat breeding crossbred cows: A comparative study
Aim: The present study was carried out to compare the associated role of micro minerals and hormones in repeat breeding animals with the normal crossbred cows.
Materials and Methods: Blood samples were collected from 10 normal cycling and 10 repeat breeding crossbred cows of Ramakrishna Mission Ashram, Narendrapur to study the plasma mineral profile and hormonal activities.
Results: Zn was found to be highly significant (p<0.01) between the two groups. Follicle stimulating hormone (FSH) and progesterone showed significant (p<0.05) difference in repeat breeding animal from the normal cyclic animal, whereas no significant differences were observed in Ca, P, Cu, Se, Co, luteinizing hormone and estradiol level.
Conclusion: It may conclude that repeat breeding condition of crossbred cows in farm condition is mainly due to the low level of progesterone, FSH and zinc