Yoshitome S , Nakamura H , Nakajo N , Okamoto K , Sugimoto I , Kohara H , Kitayama K , Igarashi K , Ito S , Sagata N , Hashimoto E .

	Fig. 1. Separation of peptides derived from dephosphorylated pp25 by reverse-phase high performance liquid chromatography (HPLC). Solid and dotted lines show absorbance at 214 nm and concentration of acetonitrile, respectively.
	Fig. 2. Nucleotide and deduced amino acid sequences of pp25 precursor protein. The putative pp25 region is boxed. The serine clusters (Ser Clu), the aminoterminal amino acid sequence reported previously (Hashimoto et al. 1995, 1996) and in Table 1 (N-ter seq), partial amino acid sequences (Pep; Table 1), and amino terminus of lipovitellin 2 (Montorzi et al. 1995) are all indicated by solid underlines. The nucleotide sequence data have been deposited in DDBJ/EMBL/ GenBank (accession number AB092605). This figure is continued on pages 287–290.
	Fig. 3. Sequence analysis of Xenopus vitellogenin B1. (a) Comparison of the predicted amino acid sequence of Xenopus vitellogenin B1 (pp25 pre) with that of chicken (Gg) vitellogenin II (Yamamura et al. 1995) and Xenopus vitellogenin A2 (Wallace et al. 1990; Plowman et al. 1994; Sunderman et al. 1995). Sequence homology (expressed as percentage identity) was determined by using the DNASIS program for each of the four putative yolk protein regions. LV, lipovitellin; PV, phosvitin; VTG, vitellogenin; YGP, york glycoprotein; pp25 pre, pp25 precursor; Xl, Xenopus laevis. (b) Comparison of the nucleotide sequence of Xenopus vitellogenin B1 (pp25 pre) with those of partial vitellogenin B1 and B2 sequences (Gerber-Huber et al. 1987; Plowman et al. 1994). Nucleotide sequences identical to those of Xenopus vitellogenin B1 are indicated by (:).
	Fig. 4. Tissue-specific expression of Xenopus vitellogenin B1. (a) Tissue-specific expression of the mRNA of Xenopus vitellogenin B1 and the housekeeping protein gene Xenopus GAPDH. Xenopus vitellogenin B1 and Xenopus GAPDH transcripts from various tissues of female Xenopus adults were analyzed by reverse transcription (RT)–polymerase chain reaction (PCR). (b) The expression of the mRNA of Xenopus vitellogenin B1 in both the ovary and the lung were detected by nested PCR. (c) Organ western blot analysis of Xenopus vitellogenin B1. A sample of protein (20 μg from stomach, kidney and ovary; 26 μg from heart; 30 μg from lung; and 40 μg from liver) from various tissues of female Xenopus adults was analyzed by western blotting by using the antipp25 antibody. The arrow on the right shows the putative position of vitellogenin B1 with molecular mass of approximately 220 000. Numbers on the left indicate the positions of molecular mass markers in kDa: 212, myosin; 170, 2-macroglobulin. (d) Induction of putative vitellogenin B1 in the liver of Xenopus treated with estrogen. A sample of liver protein (25 μg) from an untreated Xenopus female or one injected with 17-estradiol 2 weeks before analysis by western blotting by using the antipp25 antibody.