. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. BRAIN HORMONE PURIFICATION 365 Blu« D*xlran (1,000,000) f-Globulin (180,000) lovalbuminU5,000) «C-Chymotrypsin ( 22,500) Cytochrome C ( 12,400 ). Bromophenol Blue TUBE NUMBER FIGURE 7. Gel-filtration on Sephadex G-100 column of the Second Scphadex G-100 Fractions and other substances of known molecular weights. Blue dextran, bromphenol blue, and cytochrome c were measured at the wave-lengths specified in text. Blue dextran, 7-globulin, and ovalbumin exhibited similar curves so that only plotting of 7-globulin was presented.
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. BRAIN HORMONE PURIFICATION 365 Blu« D*xlran (1,000,000) f-Globulin (180,000) lovalbuminU5,000) «C-Chymotrypsin ( 22,500) Cytochrome C ( 12,400 ). Bromophenol Blue TUBE NUMBER FIGURE 7. Gel-filtration on Sephadex G-100 column of the Second Scphadex G-100 Fractions and other substances of known molecular weights. Blue dextran, bromphenol blue, and cytochrome c were measured at the wave-lengths specified in text. Blue dextran, 7-globulin, and ovalbumin exhibited similar curves so that only plotting of 7-globulin was presented. BH-I, -II, and -III indicate the Second Scphadex G-100 Fraction-I, -II, and -///, respectively. number of Sephadex used or to a slight difference in procedures. In any event, the elution pattern was satisfactorily reproducible between separate runs of identical materials, so that there must have been no defect on the estimation of the molecular weights. The approximate molecular weights of BH were thus estimated as 31,000, and 9000 for the Second Fraction-I, -II, and -///, respectively. DISCUSSION About 8000-fold purification of BH was accomplished and only of the most purified preparation, the Second Sephadex G-100 Fraction-II, as deter- mined by protein measurement, was active to cause adult development in a Samia assay pupa. The data suggested, however, that the most purified preparations were still accompanied with too many other substances. The purification procedures employed in this study were all those used routinely for protein purification and BH was successfully purified by these procedures. On the basis of this fact and inactivation of BH by some proteolytic enzymes (Ichikawa and Ishizaki, 1963), we assume that BH is a polypeptide(s) or small protein(s). Recently Kobayashi and Yamazaki (1966) obtained similar results on the protein- aceous nature of BH. Evidence for the proteinaceous nature of the neurosecretory substances in invertebr
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Keywords: ., bookauthorlilliefrankrat, booksubjectbiology, booksubjectzoology
