1958
DOI: 10.1016/0003-9861(58)90017-1
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Clostridium histolyticum collagenase: Its purification and properties

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Cited by 101 publications
(40 citation statements)
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“…One such bacterial collagenase known as Clostridium histolyticum collagenase (ChC), which belongs to the family of M-31 metalloproteinase family, is capable of hydrolyzing triple helical region of the collagen molecules under physiological conditions as well as many synthetic peptides 11,12 . The MMPs-collagenases and ChC, though relatively different, are considered to act through the same mechanism of action in the hydrolysis of collagens and collagen-like synthetic peptides [13][14][15][16] . In this study, we evaluated the protective effect of collagen by TA against collagenase degradation.…”
Section: Research Articlementioning
confidence: 99%
“…One such bacterial collagenase known as Clostridium histolyticum collagenase (ChC), which belongs to the family of M-31 metalloproteinase family, is capable of hydrolyzing triple helical region of the collagen molecules under physiological conditions as well as many synthetic peptides 11,12 . The MMPs-collagenases and ChC, though relatively different, are considered to act through the same mechanism of action in the hydrolysis of collagens and collagen-like synthetic peptides [13][14][15][16] . In this study, we evaluated the protective effect of collagen by TA against collagenase degradation.…”
Section: Research Articlementioning
confidence: 99%
“…This may involve simple breaking of hydrogen bonds as in urea treatment which results in denatured collagen susceptible to enzymes such as trypsin. However, the entire collagenase system differs from such proteinases by its specificity and complete lack of reaction with other proteins such as casein or haemoglobin as well as numerous synthetic substrates tested in this laboratory (Mandl, Zipper & Ferguson, 1957).…”
Section: Discussionmentioning
confidence: 99%
“…This may involve simple breaking of hydrogen bonds as in urea treatment which results in denatured collagen susceptible to enzymes such as trypsin. However, the entire collagenase system differs from such proteinases by its specificity and complete lack of reaction with other proteins such as casein or haemoglobin as well as numerous synthetic substrates tested in this laboratory (Mandl, Zipper & Ferguson, 1957).The presence of a specific gelatinase was first suspected when fractionation of crude collagenase (DeBellis el aZ. 1954) invariably showed the fraction with maximum collagenase activity preceding the corresponding azocoll maximum, If the collagenase were the only enzyme in this region capable of attacking azocoll, the maxima should coincide.…”
mentioning
confidence: 99%
“…За одиницю фібриногенолітичної активності брали таку кількість ензиму, яка підвищує оптичну густину реак-ційної суміші на 0,01 за 1 хв. Колагеназну активність визначали за методом [10]. Продукти розщеплення колагену визначали в реакції з нінгідрином на спектрофотометрі СФ-26 при довжині хвилі 600 нм.…”
Section: матеріали та методиunclassified
“…Визначення активності пептидаз щодо синтетичних субстратів про-водили за методом [10]. Концентрація відщепленого в результаті реакції пара-нітроаніліду (pNA) пропорційна активності пептидази і визначається за збільшенням поглинання при довжині хвилі 405-410 нм.…”
Section: матеріали та методиunclassified