ISOLATION, PURIFICATION AND ANTI-BACTERIAL PROPERTY OF CALPROTECTIN FROM BOVINE NEUTROPHIL

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

IMANI M.; TOUKMECHI A.

Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Journal of Veterinary Research Year:2016 | Volume:71 | Issue:1 Page(s): 57-64

Download Full-Text

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Verion

View:

801

Download:

Cites:

Information Journal Paper

Title

ISOLATION, PURIFICATION AND ANTI-BACTERIAL PROPERTY OF CALPROTECTIN FROM BOVINE NEUTROPHIL

Author(s)

IMANI M. | TOUKMECHI A. | Issue Writer Certificate

Keywords

ANTIBACTERIAL ACTIVITYQ1

ISOLATIONQ1

NEUTROPHILQ2

P7/P23Q1

Abstract

BACKGROUND: It is believed that bovine NEUTROPHILs contain several peptides and protein which exhibit antimicrobial activity against microorganisms such as fungi and bacteria.OBJECTIVES: The purpose of this study was to isolate and purify a potential antibacterial protein from bovine NEUTROPHIL and test its anti bacterial activity.METHODS: NEUTROPHILs were isolated from bovine blood using dextran sedimentation and centrifugation on Ficoll-Hypaqe. Cell viability is examined by trypan blue dye exclusion method. Protein extract was then dialyzed and applied onto ion exchange chromatography for further purification, and its potential cytostatic activity was examined against Staphylococcus aureus, Aeromonas hydrophila and Yersinia ruckeri.RESULTS: Viability of isolated NEUTROPHIL was over 95%, chromatographic results and SDS-PAGE analysis exhibited that NEUTROPHIL cytosolic proteins were fractionated so that the purification of P7/P23 was almost 60% in the first step and purification was completed in the second phase. Using calibration curve according to molecular mass markers, the relative molecular mass of P7 and P23 determined as 7 kDa and 23 kDa, respectively. Also, results showed that this protein has ANTIBACTERIAL ACTIVITY and has higher bactericidal activity against Y. ruckeri.CONCLUSIONS: It could be concluded that purification of P7/P23 sustains its biological activity and has wide range ANTIBACTERIAL ACTIVITY. Moreover, taking all data into account may suggest that the cytostatic activity of NEUTROPHIL, to some extent, results from P7/P23 protein which is abundant in the cytosole.

Cites

No record.

References

No record.

Cite

APA: Copy

IMANI, M., & TOUKMECHI, A.. (2016). ISOLATION, PURIFICATION AND ANTI-BACTERIAL PROPERTY OF CALPROTECTIN FROM BOVINE NEUTROPHIL. JOURNAL OF VETERINARY RESEARCH, 71(1), 57-64. SID. https://sid.ir/paper/34855/en

Vancouver: Copy

IMANI M., TOUKMECHI A.. ISOLATION, PURIFICATION AND ANTI-BACTERIAL PROPERTY OF CALPROTECTIN FROM BOVINE NEUTROPHIL. JOURNAL OF VETERINARY RESEARCH[Internet]. 2016;71(1):57-64. Available from: https://sid.ir/paper/34855/en

IEEE: Copy

M. IMANI, and A. TOUKMECHI, “ISOLATION, PURIFICATION AND ANTI-BACTERIAL PROPERTY OF CALPROTECTIN FROM BOVINE NEUTROPHIL,” JOURNAL OF VETERINARY RESEARCH, vol. 71, no. 1, pp. 57–64, 2016, [Online]. Available: https://sid.ir/paper/34855/en

Related Journal Papers