The preparation of soft-tritium-labelled proteins and their application for the collagenolytic activity investigations.
Tritium-labelled Type I collagen from rat skin with specific activity of 8 mCi/mg and mixture of the crab hepatopancrease collagenolytic enzymes with specific activity of 25 mCi/mg have been obtained by the method of high-temperature solid-state catalytic isotope exchange (HSCIE) without loss of native features. Tritium-labelled Type I collagen kept its ability to form native fibrils being resistant to trypsin hydrolysis. Tritium-labelled collagenase keeps about 70% of its proteolytic activity.
Klimova
O A
OA
Institute of Molecular Genetics, Russia Academy of Sciences, Moscow.
Zolotarev
Y A
YA
Chebotarev VYu
D000818:Animals; D003386:Brachyura; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000378:metabolism*; D017364:Collagenases / Q000302:isolation & purification / Q000378:metabolism*; D004064:Digestive System / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D007553:Isotope Labeling / Q000379:methods; D051381:Rats; D012867:Skin / Q000378:metabolism; D014316:Tritium
D007527:Isoenzymes; D014316:Tritium; D003094:Collagen; D017364:Collagenases