The specificity of a monoclonal antibody raised to human titin was characterized. The antibody reacts with an epitope which is common to titin and the high mol. wt subunits NF-H and NF-M of mammalian neurofilaments. 2. 2. Mapping of the epitope indicated that it is located in the carboxyterminal extension of NF-H and NF-M, and that its reactivity does not depend on the phosphorylation state of the molecule. 3. 3. A comparative study on neurofilament protein of lower vertebrates revealed that this epitope has been conserved during vertebrate evolution.
Mencarelli, C., Magi, B., Marzocchi, B., Armellini, D., Pallini, V. (1991). Evolution of the "titin epitope" in neurofilament proteins. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. B, COMPARATIVE BIOCHEMISTRY, 100(4), 741-744 [10.1016/0305-0491(91)90283-J].
Evolution of the "titin epitope" in neurofilament proteins.
MENCARELLI, CATERINA;MAGI, BARBARA;MARZOCCHI, BARBARA;PALLINI, VITALIANO
1991-01-01
Abstract
The specificity of a monoclonal antibody raised to human titin was characterized. The antibody reacts with an epitope which is common to titin and the high mol. wt subunits NF-H and NF-M of mammalian neurofilaments. 2. 2. Mapping of the epitope indicated that it is located in the carboxyterminal extension of NF-H and NF-M, and that its reactivity does not depend on the phosphorylation state of the molecule. 3. 3. A comparative study on neurofilament protein of lower vertebrates revealed that this epitope has been conserved during vertebrate evolution.
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https://hdl.handle.net/11365/49607