Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus).
作者： Michael Reith , Janet Munholland , John Kelly , Roderick Nigel Finn , Hans J�rgen Fyhn
DOI: 10.1002/JEZ.5
关键词:
摘要: In the process of cloning vitellogenin (Vtg) cDNAs from haddock (Melanogrammus aeglefinus), two related, but distinct, mRNAs were identified. Full-length cDNA sequences de- termined for both Vtg types (Had1 and Had2), deduced amino acid found to be 54% identical each other 48-58% teleost Vtgs. To investigate expres- sion mRNAs, proteins prehydrated oocytes fertilized eggs separated on SDS-polyacrylamide gels. Only a single lipovitellin I band was detected in sample, egg smaller (97 vs. 110 kDa) than oocyte protein, indicative proteolytic processing during hydration. Mass spectrometric (MALDI-TOFMS tandem mass spectrometry) analy- ses tryptic fragments revealed that contained matched Vtg, suggesting there this band, while only Had1 sequence, indicating Had2 had been degraded Physiological data demonstrate that, as marine fish spawn pelagic eggs, free content increases hydration apparently contributes by driving osmotic uptake water. The correlation disappearance one with increase acids suggests protein is major source J. Exp. Zool. (Mol. Dev. Evol.) 291:58-67, 2001. © 2001 Wiley-Liss, Inc.
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