Collagen type II, alpha 1 protein: A bioactive component of shark cartilage

Merly, Liza; Smith, Sylvia L.

doi:10.1016/j.intimp.2012.12.001

Cited by 25 publications

(16 citation statements)

References 23 publications

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“…Stabilization of collagen helix is more likely to occur primarily by intermolecular rather than intra-molecular association, which thus increases thermal properties (Montero and Gomez-Guillen 2000) The T d of CII (34.02°C) was higher than that of CIIp (21.5°C). The T d of other fish and calf collagen ranged from 19.4 to 40.8°C (Merly and Smith 2013;Kittiphattanabawon et al 2010;Muyonga et al 2004;Wang et al 2014). In the present study, the Td of collagen was quite higher than those reported for skin collagen of allied teleosts such as cod (15°C) and carp (28°C) (Duan et al 2009;Sadowska et al 2003).…”

Section: Maximum Absorbancecontrasting

confidence: 73%

“…Glycoprotein/carbohydrate estimation Purified collagen samples were examined for carbohydrate content using the glycoprotein/carbohydrate estimation kit (Thermo Scientific Catalog #23260) (Merly and Smith 2013). All samples were diluted to 0.25 and 2.5 mg/ml protein in glycoprotein assay buffer.…”

Section: Protein Patternmentioning

confidence: 99%

“…It was evident that the carbohydrate contents of collagen isolated from commercial shark cartilage capsules were between 5 and 40 % (Merly and Smith 2013). Backlund et al (2002) opined that glycoprotein content of CII is a key element for the recognition of T cell in collagen-induced arthritis models.…”

Section: Glycoprotein/carbohydrate Contentmentioning

confidence: 99%

“…Backlund et al (2002) opined that glycoprotein content of CII is a key element for the recognition of T cell in collagen-induced arthritis models. Recently, Merly and Smith (2013) studied the effect of oral administration of fetal bovine articular cartilage collagen for the treatment of RA. In the present study, the higher content of glycoprotein showed that the purified CIIp could be used as a novel drug to treat RA.…”

Section: Glycoprotein/carbohydrate Contentmentioning

confidence: 99%

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Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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A low molecular weight type-II collagenous polypeptide (CIIp) from whale shark (WS) cartilage was prepared by thermolysin digestion; and examined for their physico-functional and antioxidant properties. The purified collagen was composed of an identical (α 1 ) 3 chains and was characterized as type-II. After hydrolysis with thermolysin, the α-chain of the WS collagen was degraded into smaller peptides with molecular weight ranging from 70 to 20KDa. CIIp was successfully separated from the hydrolysates with molecular weight of approximately 37 kDa. Amino acid analysis of CII, and CIIp indicated imino acid contents of 155 and 121 amino acid residues per 1000 residues, respectively. Differing Fourier transform infrared (FTIR) spectra of CII and CIIp were observed, which suggested that the hydrolysis process by thermolysin affected the secondary structure and molecular order of collagen, particularly the triple-helical structure. The denaturation temperature of CII (34°C) was higher than that of CIIp. Low content of glycoprotein was observed in CII than CIIp due to removal of some polypeptides by thermolysin digestion. The antioxidant activity against 1,1-diphenyl-2-picrylhydrazyl radicals and the reducing power of CIIp was greater than that of CII. The results proposed that the purified CIIp from WS cartilage with excellent antioxidant activities could be the suitable biomaterial for therapeutic applications.

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Section: Maximum Absorbancecontrasting

confidence: 73%

Section: Protein Patternmentioning

confidence: 99%

Section: Glycoprotein/carbohydrate Contentmentioning

confidence: 99%

Section: Glycoprotein/carbohydrate Contentmentioning

confidence: 99%

See 2 more Smart Citations

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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show abstract

“…Purified collagen samples were examined for carbohydrate content using the glycoprotein/carbohydrate estimation kit (Thermo Scientific Catalog #23260) [18]. All samples were standardized to 0.25 and 2.5 mg/mL protein in glycoprotein assay buffer.…”

Section: Glycoprotein/carbohydrate Estimationmentioning

confidence: 99%