Wakata Y , Tokumoto M , Horiguchi R , Ishikawa K , Nagahama Y , Tokumoto T .

	Figure 1. Amino acid sequence comparison of the Xenopus, human, Drosophila, and Yeast α1, α5 and α6 proteasome subunits. Amino acid sequence comparisons of α1 (A), α5 (B) and α6 (C) proteasome subunits are indicated. Matched sequences are boxed. Consensus sequences for calcium/calmodulin-dependent kinase II (CaMKII), cAMP/cGMP-dependent kinase (cAMP/cGMP), casein kinase II (CKII) and Ca2+-dependent kinase (PKC) are indicated. The numbers refer to the amino acid position at the end of each line.
	Figure 2. Amino acid sequence comparison of the Xenopus proteasomal α subunits. Matched sequences are boxed. The proteasomal α-type and β-type signatures were detemined by using the 'PROSITE' database [17] and are boxed. The numbers refer to the amino acid position at the end of each line.
	Figure 3. Immunoblotting of the cytosol fraction and purified 26S proteasome. The cytosol fraction and purified 26S proteasome were electrophoresed under denaturing conditions (10.0% gel) and stained with Coomassie Brilliant Blue (CBBR), or immunostained with antibodies for α subunits of the 20S proteasome. Lanes cyt and 26S indicate the cytosol fraction and the 26S proteasome from immature oocytes, respectively. Molecular masses of standard proteins are indicated at the left. Protein bands of each subunit are indicated by arrows.
	Figure 4. 2D-PAGE analysis of 26S proteasomes from immature and mature oocytes. The 26S proteasomes from immature (I) and mature (M) oocytes were subjected to 2D-PAGE followed by immunostaining with polyclonal antibodies against each of the Xenopus 20S proteasome subunits as indicated. The spots detected by each antibody are represented at high magnification and indicated by arrows. The spots differing between immature and mature oocytes are indicated by asterisks.

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