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Gelatinase enzymes can be found in a number of eukaryotes, including mammals, and birds; bacteria including Pseudomonas aeruginosa and Serratia marcescens), and fungi, but may have variations among species based on identification and function of the gelatinase type. In humans, the gelatinases expressed are matrix metalloproteinases MMP2 and ...
Gelatin is a collection of peptides and proteins produced by partial hydrolysis of collagen extracted from the skin, bones, and connective tissues of animals such as domesticated cattle, chicken, pigs, and fish. During hydrolysis, some of the bonds between and within component proteins are broken.
17395 Ensembl ENSG00000100985 ENSMUSG00000017737 UniProt P14780 P41245 RefSeq (mRNA) NM_004994 NM_013599 RefSeq (protein) NP_004985 NP_038627 Location (UCSC) Chr 20: 46.01 – 46.02 Mb Chr 2: 164.78 – 164.8 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Matrix metalloproteinase-9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), is a ...
This group of metallopeptidases constitutes the MEROPS peptidase family M9, subfamilies M9A and M9B (microbial collagenase, clan MA(E)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH.
Collagen proteins are often associated with the strengthening and support of many tissues including skin, bones, muscles, and ligaments. There are some studies that suggest that Type V collagen is responsible for the formation of other collagen fibrils in different tissues within the body. [ 3 ]
Baculovirus-infected insect cells [20] (Sf9, Sf21, High Five strains) or mammalian cells [21] (HeLa, HEK 293) allow production of glycosylated or membrane proteins that cannot be produced using fungal or bacterial systems. [20] [6] It is useful for production of proteins in high quantity. Genes are not expressed continuously because infected ...
The gelatinases are No. 2 and No. 9. The stromelysins display a broad ability to cleave extracellular matrix proteins but are unable to cleave the triple-helical fibrillar collagens. The three canonical members of this group are No. 3, No. 10, and No. 11.
The MMP family is formed by twenty related zinc-dependent enzymes. They are noted for having the ability to degrade extracellular matrix proteins, such as collagens, laminin, and proteoglycans. These calcium- and zinc-dependent proteases are activated at neutral pH and twenty-three have been found present in mammalian cells.