Gel electrophoresis of soluble and insoluble proteins of noradrenergic vesicles from ox splenic nerve: a comparison with proteins of adrenal chromaffin granules.
Polyacrylamide gel electrophoresis of a soluble extract of purified large dense-cored vesicles (noradrenergic vesicles) from ox splenic nerve revealed 13 proteins, 7 of which had mobilities close to those of seven of the soluble proteins in adrenal chromaffin granules. Two of these proteins had the same mobilities as dopamine beta-hydroxylase and chromogranin A, respectively. The relative staining intensities of the latter two proteins were different: in noradrenergic vesicles, there was more dopamine beta-hydroxylase than chromogranin A; whereas in chromaffin granules, chromogranin A was the major protein. Gel electrophoresis of the water-insoluble proteins of noradrenergic vesicles, dissolved in sodium dodecylsulphate, revealed 5 proteins, 5 of which had mobilities close to those of 5 proteins present in the membranes of chromaffin granules. Three of these proteins had mobilities similar to those of dopamine beta-hydroxylase, chromogranin A and chromomembrin B, respectively. One of the proteins was probably serum albumin, which was also present as a contaminant in the soluble extract of noradrenergic vesicles. These findings are consistent with earlier studies in which dopamine beta-hydroxylase, chromogranin A and chromomembrin B have been identified as constituents of noradrenergic vesicles by enzymatic or immunochemical assay methods. They also indicate further qualitative similarities between the noradrenergic vesicle and the chromaffin granule, in that a total of 7 soluble and 5 insoluble proteins might be common to both particles. However, gel electrophoresis also confirms that quantitative differences exist between the relative proportions of the soluble proteins and shows that dopamine beta-hydroxylase is the major soluble protein of the noradrenergic vesicles isolated from splenic nerve trunks.
Bartlett
S F
SF
Department of Pharmacology, University of Oxford, Oxford OX1 3QT, England.
Lagercrantz
H
H
Smith
A D
AD
D000313:Adrenal Medulla / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D002837:Chromaffin Granules / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D009419:Nerve Tissue Proteins / Q000302:isolation & purification* / Q000378:metabolism; D009638:Norepinephrine / Q000378:metabolism*; D017729:Presynaptic Terminals / Q000378:metabolism*; D012995:Solubility; D013154:Spleen / Q000294:innervation*; D017779:Sympathetic Fibers, Postganglionic / Q000378:metabolism*; D013572:Synaptic Vesicles / Q000378:metabolism*
D009419:Nerve Tissue Proteins; D009638:Norepinephrine