| pubmed-article:2793524 | pubmed:abstractText | Antisera were raised against synthetic peptides derived from the primary amino acid sequence of human chromogranin B. These antisera recognized in one- and two-dimensional immunoblotting a component previously designated as chromogranin B. In human chromaffin granules, the major endogenous processing product of chromogranin B is formed by proteolytic cleavage of the protein near the C-terminus. Immunohistochemical localizations were obtained with antisera against human chromogranins A and B and against a synthetic peptide corresponding to the B sequence. In human tissues, chromogranin B is co-stored with chromogranin A in the adrenal medulla, the anterior pituitary, parafollicular cells of the thyroid, in some cells of the endocrine pancreas and in some enterochromaffin cells, whereas only chromogranin A is found in the parathyroid gland and enterochromaffin cells of the gastric corpus mucosa. In the nervous system, no immunostaining was observed for chromogranin A and only a weak one for chromogranin B in some cells of the spinal cord. However, the Purkinje cells of the cerebellum were strongly positive for chromogranin B. | lld:pubmed |
