Abstract
The effects of enhancement of enzymatic activity by heating at 56°C or by limited treatment with dimethylsulfoxide, trypsin and cathepsin d on two forms (Mr = 50 kDa and 72 kDa) of human epidermal transglutaminase were studied by immunoblots using rabbit antihuman epidermal transglutaminase. Both 50 kDa and 72 kDa transglutaminase bands were detected without any alteration in the mobility of the transglutaminase bands during activation induced by heating at 56°C or by pretreatment with dimethylsulfoxide. With a preincubation period longer than 60 min, the trypsin pretreated sample showed progressive disappearance of the 72 kDa transglutaminase band in conjunction with the loss of transglutaminase activity. On the other hand, samples preincubated with cathepsin d showed a complete disappearance of the 50 kDa band after 180 min. These studies suggest the different forms of human epidermal transglutaminase may regulate enzyme activity each other during normal epidermal differentiation.
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