4 research outputs found

    Online) An Open Access

    Get PDF
    ABSTRACT The present study was conducted to analyze the MMP activity in the serum of Giriraja fowl. Blood was collected from six male and six female healthy Giriraja fowls and serum was separated and stored at -20 O C until further use. The serum samples were subjected to Gelatin zymography. A prominent band of 72 kDa (proform), and active form of MMP-2 (62 kDa) were observed. Only one bands observed in both male and female, serum samples. Among these 2 bands, proform of MMP-2 was showing greater gelatinolytic activity. The ratio of proMMP-2/active MMP-2 was found to be 4. None of 3 isoforms of MMP-9 (92,135,220 kDa) was found in the gel in both cock and hen serum samples

    Comparative study on serum matrix metalloproteinases in various species of domestic animals

    Get PDF
    A study was conducted to evaluate the presence of matrix metalloproteinases (MMP) in the serum of domestic animal species. The serum samples were collected from four healthy male animals of each species, viz. goat, cattle, horse, rabbit, sheep, pig and 4 tumor affected dogs in a heparinzed vacutainer, during early morning before feeding the animals. All the serum samples were subjected to gelatin zymography. The major bands were observed at 220, 92 kDa of MMP-9 and 72 kDa of MMP-2 in all the species with minor variations in rabbit and goat. It was observed that these bands indicated the normal physiological state of the animals and in tumour samples, the intensity of both MMP-9 and MMP-2 was 2–3 times higher. The level of expression of latent form of MMP-9 band was comparable in goat, cattle, horse, sheep and pig and also they were as expressed in human, on contrast there was low level of expression in rabbit as it clearly indicated these MMP proteins were in low concentration in the serum of rabbit. The thickness of Pro-MMP-9 (92 kDa) band in horse serum was alike as in the human marker and it might be related to human protein. There was a faded band below 72 kDa band in all the species but it was absent in human serum as it could be the active form of MMP-2 (62 kDa). MMP-2 band in cattle and horse serum were correlated. The concentration of the MMP-2 band in sheep serum was higher than in the other species used in this study but it was lesser than the activity of protein isolated from canine tumor. It was concluded that MMP plays a significant role in normal physiological functions of every species and its activity was 4–5 times higher in tumor samples due to greater gelatinolytic activity. Thus, it was concluded that tumor samples exhibit greater gelatinolytic activity because of higher concentration of MMP proteins

    MOLECULAR CHARACTERIZATION OF MMP-9 GENE IN CYSTIC FLUID OF CYSTICERCUS TENUICOLLIS BY REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION (RT-PCR)

    Get PDF
    ABSTRACT The present study was carried out to confirm the presence of MMP-9 gene in the cystic fluid of Cysticercus tenuicollis. Collection of cyst was made from goats slaughtered at local abattoirs and washed thoroughly with PBS (pH 7.4). The cystic fluid was aspirated, centrifuged at 10,000 rpm for 15 minutes at 4°C and the supernatants were used for further study. Total RNA was isolated from the cystic fluid of Cysticercus tenuicollis. The total cellular RNA was obtained from 400 µL of cystic fluid was 0.214 µg and the concentration of the RNA was 0.535 µg/mL. The RT-PCR product, 204 bp propeptide domain of MMP-9 was detected through agarose gel electrophoresis, which confirmed the presence of MMP-9 in the cystic fluid of Cysticercus tenuicolli

    Not Available

    No full text
    Not AvailableThe present study was undertaken to assess the effect of bovine serum albumin (BSA) on sperm motility, viability, total spermabnormality, acrosomal and plasmamembrane integrity. A total of 30 ejaculates were collected from mithun bulls and semen was split into five equal aliquots, diluted with the TEYC extender. Group 1: semen without additives (control), group 2 to group 4: semen was diluted with 5 mg/ml, 10 mg/ml and 20 mg/ml of BSA, respectively. These seminal parameters were assessed at 5oC for 0, 6, 12, 24 and 30 h of incubation. Inclusion of BSA into diluent resulted in significant (P <0.05) decrease in percentages of dead spermatozoa, abnormal spermatozoa and acrosomal abnormalities at different hours of storage periods as compared with control group.Additionally, BSAat 5mg/ml has significant (p< 0.05) improvement in quality of semen than BSA at 10 mg/ml and 20 mg/ml stored in in-vitro for up to 30 h. It was concluded that the possible protective effects of BSA on sperm parameters may be due to the prevention of lipid peroxidation.Not Availabl
    corecore