caa a22 4500 475744489 CHVBK 20180406123509.0 cr unu---uuuuu 170329e20000701xx s 000 0 eng 10.1023/A:1026487414167 doi (NATIONALLICENCE)springer-10.1023/A:1026487414167 Subunit Composition of the Zinc Proteins α- and β-Lipovitellin from Chicken [Elektronische Daten] [Dieter Groche, Leonid Rashkovetsky, Kenneth Falchuk, David Auld] Chicken α- and β-lipovitellin are derived from parent vitellogenin proteins and contain four subunits (125, 80, 40, and 30 kDa) and two subunits (125 and 30 kDa), respectively. Metal analyses demonstrate both are zinc proteins containing 2.1 ± 0.2 mol of zinc/275 kDa per α-lipovitellin and 1.4 ± 0.2 mol of zinc/155 kDa per β-lipovitellin, respectively. The subunits of β-lipovitellin, Lv 1 (MW 125 kDa) and Lv 2 (MW 30 kDa), are separated by gel exclusion chromatography in the presence of zwittergent 3-16. Zinc elutes with Lv 1, suggesting that this subunit binds zinc in the absence of Lv 2. The subunits of α- and β-lipovitellin were separated by SDS-PAGE, digested with trypsin, and mapped by reverse-phase HPLC. The peptide maps of the 125-kDa subunits from α- and β-lipovitellin are essentially identical. Similar results are obtained for the 30-kDa subunits of both lipovitellins. The sequences of five and four peptides of the 125-kDa subunit of α- and β-Lv, respectively, and two peptides of the 30-kDa subunit of α- and β-lipovitellin were determined and match those predicted from the gene for vitellogenin II, Vtg II. Comparison of the amino acid composition of the 125- and 30-kDa subunits of α- and β-lipovitellin support the conclusion that they originate from the same gene. The sequences of peptides from the 80- and 40-kDa subunits of α-lipovitellin have not been found in the NCBI nonredundant data bank. The 27-amino acid N-terminal sequence of the 40-kDa protein is 56% similar to the last third of the Lv 1-coding region of the Vtg II gene, suggesting it may come from an analogous region of the Vtg I gene. We propose a scheme for the precursor—product relationship of Vtg I. Plenum Publishing Corporation, 2000 Vitellogenin nationallicence embryogenesis nationallicence chicken nationallicence zinc storage protein nationallicence Groche Dieter Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut Rashkovetsky Leonid Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut Falchuk Kenneth Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut Auld David Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/5(2000-07-01), 379-387 0277-8033 19:5<379 2000 19 10930 https://doi.org/10.1023/A:1026487414167 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1026487414167 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Groche Dieter Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut NATIONALLICENCE 700 1- Rashkovetsky Leonid Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut NATIONALLICENCE 700 1- Falchuk Kenneth Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut NATIONALLICENCE 700 1- Auld David Center for Biochemical and Biophysical Sciences and Medicine, Brigham and Women's Hospital, Boston, Massachusetts aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/5(2000-07-01), 379-387 0277-8033 19:5<379 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer