A calpain-like proteolytic activity produces the limited cleavage at the N-terminal regulatory domain of rabbit skeletal muscle AMP deaminase: evidence of a protective molecular mechanism.

Martini, D; Montali, U; Ranieri-Raggi, M; Sabbatini, A R M; Thorpe, S J; Moir, A J G; Raggi, A

Martini, D; Montali, U; Ranieri-Raggi, M; Sabbatini, A R M; Thorpe, S J; Moir, A J G; Raggi, A.

Affiliation

Martini D; Dipartimento di Scienze dell'Uomo e dell'Ambiente, Chimica e Biochimica Medica, Università di Pisa, Via Roma 55, 56126 Pisa Italy.

Biochim Biophys Acta ; 1702(2): 191-8, 2004 Nov 01.

Article in En | MEDLINE | ID: mdl-15488771

Subject(s)

AMP Deaminase/chemistry; AMP Deaminase/metabolism; Calpain/metabolism; Muscle, Skeletal/enzymology; AMP Deaminase/genetics; Animals; Calpain/antagonists & inhibitors; Enzyme Activation; Humans; Peptides/genetics; Peptides/metabolism; Rabbits

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Collection: 01-internacional Database: MEDLINE Main subject: Calpain / Muscle, Skeletal / AMP Deaminase Limits: Animals / Humans Language: En Journal: Biochim Biophys Acta Year: 2004 Type: Article

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