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Current IssueEditorial BoardOnline First Articles
Indian Journal of
Animal Research
Print ISSN: 0367-6722
Online ISSN: 0976-0555
NASS Rating
6.40
SJR
0.233
CiteScore
0.606

Chief Editor:
M. R. Saseendranath
Kerala Veterinary and Animal Science University, Mannuthy, Thrissur, INDIA
Frequency:Monthly
Indexing:
Science Citation Index Expanded, BIOSIS Preview, ISI Citation Index, Biological Abstracts, Scopus, ...

Indian Journal of Animal Research, volume 49 issue 1 (february 2015) : 127-131

Isolation and characterization of Stromelysin-3(MMP-11) like protein from a case of mammary carcinoma in a dog

Sujata Sahoo*, Meena Kataria, S.K. Maiti
1Division of Animal Biochemistry Indian Veterinary Research Institute, Izatnagar, Bareilly-243 122, India.
Cite article:- Sahoo* Sujata, Kataria Meena, Maiti S.K. (2025). Isolation and characterization of Stromelysin-3(MMP-11) like protein from a case of mammary carcinoma in a dog. Indian Journal of Animal Research. 49(1): 127-131. doi: 10.5958/0976-0555.2015.00026.6.

ABSTRACT

Stromelysin-3(MMP-11) is a matrix-metalloproteinase known to be over expressed in invasive tumors of human origin and suppose to have a potential role in metastasis. Dog mammary tumors are usually very invasive. Thus to characterize dog stromelysin-3, mammary tumor tissue (papillary adenocarcinoma) was used to isolate the protein by using affinity chromatography tools including Cibacron-Blue 3GA-CL Agarose, gelatin Sepharose, and  heparin Sepharose columns. Western blotting with antihuman stromelysin-3 antibody was done for identification. The result showed a heavier (120kDa) protein than the expected size of stromelysin-3. Western blot analysis of the crude sample did not show any other reactive bands. Under reducing condition, the protein size remained intact. The stromelysin-3 like protein showed mild caseinolytic activity, which increased by activators like APMA and trypsin. Whereas, its activity decreased when inhibitors like EDTA, 1, 10-Phenanthroline and TIMP-1 were used suggesting the requirement of calcium and zinc for enzyme activity just like any other metalloproteinase.

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