Abstract
Immunoreactive related CGRP molecules (ir-CGRP) were identified in the abalone, Haliotis tuberculata, mainly in mantle and cephalic part extracts. Ir-CGRP in both tissues accounted for 461 and 455.6 pg per mg of proteins, respectively. These CGRP-immunoreactive molecules were further analyzed for their ability to interact with the CGRP radioreceptor assay. In specific target tissues for CGRP (rat liver membranes), 50% inhibition of 125I-labeled CGRP specific binding was observed with 4.7 μg and 21.1 μg of proteins from mantle and cephalic part extract, respectively. These molecules were submitted to gel-filtration chromatography on a Sephacryl S-100 column and were further analyzed in the radioreceptor assay specific for CGRP. The elution position of these molecules suggested a molecular weight close to that of synthetic salmon calcitonin.
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