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Comparison of nonstructural glycoprotein NSP4 gene sequences from 22 rotavirus strains originating from six host species and of 14 different combinations of G and P types revealed the presence of three distinct NSP4 alleles, represented by strains Wa, KUN and AU-1. Genetic distances between any of these alleles (18n0 %) were significantly greater than those within each allele (5n5 %) and phylogenetic analysis suggested that divergence into three distinct alleles had occurred at about the same time during evolution. While amino acid variation among strains was minimal in the amino-

Portal vein aneurysm is very rare, and its relation to portal hypertension has been emphasized. We report six cases of portal vein aneurysm (five extrahepatic and one intrahepatic). All patients were asymptomatic and had no signs suggestive of portal hypertension; the lesion was incidentally detected by ultrasound. Color Doppler sonography showed a constant hepatopetal flow along the aneurysmal wall, which immediately led to the diagnosis. We stress the usefulness of color Doppler sonography for studying the hemodynamics of this vascular anomaly and briefly review the literature.

Mammalian chaperonin homolog (HSP60) was purified from porcine livers cytosol using a tandem ATP-Sepharose column and Mono Q column chromatography. A partial amino acid sequence (96 amino acid residues) of this protein was determined and coincided with those of human HSP60 with 96.9% homology, which was deduced from the nucleotide sequence of the cDNA. The sequence of the NH2 termini of the purified protein (5 amino acid residues) coincided with the signal sequence of HSP60. These facts led to the identification of the 60-kDa liver protein with the chaperonin homolog. Dihydrofolate reductase was able to form a stable complex with the liver chaperonin homolog. The liver chaperonin homolog was detected by at least five spots around pI = 5.6 on two-dimensional gel electrophoresis. Immunoblotting studies using an antibody against chaperonin homolog showed that the chaperonin homolog was localized in the cytosol, mitochondrial, and nuclear fractions of porcine liver. The chaperonin homolog was localized both in the mitochondria and cytoplasm of rat kidneys at the electron microscopic level. The chaperonin homolog in the cytosol, but not in the other subcellular fractions, was cross-reacted with an antibody against the synthetic peptide corresponding to the signal peptide of HSP60 as well as the purified chaperonin homolog on immunoblotting. These results suggested that the functional chaperonin homolog in the cytosol may be transported into the mitochondria and the protein may be processed to mitochondrial HSP60 in the organella.

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