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Biomedical subjects

F Ichida

Publications and source records attributed to F Ichida.

At least 109 records · Page 6Linked to original sources
PubMed1981

Propagation of human hepatitis A virus in conventional cell lines.

Fecal extracts of hepatitis A (HA) patients were selected for the presence of hepatitis A virus (HAV) by radioimmunoassay (RIA) and immune electron microscopy (IEM). When FL and Vero cells were inoculated with fecal extracts containing HAV, development of hepatitis A antigen (HAAg) was evident in the cytoplasm of the two cell lines by the indirect immunofluorescence (IF) test. The antigen was detectable in the cells 12 hr postinoculation (pi), and reached a plateau within two days pi. FL cell cultures inoculated with a specimen containing HAV were harvested and passaged four times. During the passages, efficient production of HAAg was confirmed in the infected cultures by three different serological tests: The indirect IF test, RIA using fixed cells, and RIA by the sandwich method. At the second and fourth passages, HAV particles were recovered in abundance from infected FL cell cultures by IEM. Throughout these experiments, no cytopathic effect (CPE) was discernible in the cultures.

Antigens, Viral↗
PubMed1981

Age specific prevalence of anti HA in Japan--from multi-institutional analysis.

In order to estimate age specific prevalence of Anti HA in Japan, 1757 serum samples from healthy subjects or patients with nonhepatic disease taken in 6 different districts of Japan were tested for Anti HA using HAVAB Kit. Very low prevalence, less than 10%, was observed in young adults or children. These facts indicate the young Japanese are quite susceptible to HAV infection and the effective preventive measures are urgently needed. Over all prevalence of Anti HA was 56.2%. Comparing the age specific prevalence of Anti HA in Japan with those in other countries, the situation in Japan was in intermediate between highly endemic South-East region and developed European countries.

Adolescent↗
PubMed1981

Distribution of fibronectin in fibrotic human livers at various states.

Fibronectin was isolated from human plasma by affinity chromatography with gelatin-coupled Sepharose 4B. Anti-fibronectin antiserum was prepared using rabbits, and human liver biopsy specimens at various stages of fibrosis were investigated for distribution of fibronectin by the indirect immunofluorescence technique. Fibronectin was absent in liver parenchymal cells, while it was detected markedly in reticulin and the area containing collagen fibers. The existence of fibronectin in the necrotic area and in prematured fibers suggests the earlier deposition of fibronectin than that of collagen at the locus of tissue repairing, and thus the important role of fibronectin at the early stage of fibrosis.

Fibronectins↗
PubMed1979

alpha-Fetoprotein as a carrier protein in plasma and its bilirubin-binding ability.

The bilirubin-binding ability of human alpha-fetoproteins, which were purified from fetal cord serum and from ascites fluid of a hepatoma-bearing patient, was examined by the difference spectrum and the Jacobsen peroxidase methods. The difference spectrum observed as a result of the specific binding of bilirubin to alpha-fetoprotein had a maximum at 482 nm, and this pattern was quite similar to that observed for serum albumin. The result obtained by the difference spectrum method showed that 1 mol of each alpha-fetoprotein bound 1 mol of bilirubin at pH 8.3 and that the dissociation constants of the complexes of bilirubin with fetal alpha-fetoprotein and hepatoma-derived alpha-fetoprotein were 2.6 x 10(-7) and 5.0 x 10(-7) M, respectively. The Jacobsen enzymatic method using horseradish peroxidase gave the same values for molar binding ratios and similar dissociation constants, 7.1 x 10(-7) M for fetal alpha-fetoprotein and 7.4 x 10(-7) M for hepatoma-derived alpha-fetoprotein. These results indicate that alpha-fetoprotein may function as a carrier protein for bilirubin as has been shown for serum albumin.

Bilirubin↗
PubMed1978

[HBsAg carrier].

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Carrier State↗
PubMed1978

Copper(II)-binding ability of human alpha-fetoprotein.

The copper(II)-binding ability of human alpha-fetoproteins, which were purified from umbilical cord serum and from ascites fluid of a hepatoma-bearing patient, was examined by equilibrium dialysis and gel filtration methods. The pH dependence of the copper(II)-binding ability of alpha-fetoprotein was quite similar to that of albumin. Alpha-fetoprotein bound 1 mol of copper(II) ion per mol of protein above pH 6.0 and 0.5 mol of copper(II) ion at pH 5.4, which is close to the pK value of the imidazole group of histidine. Photooxidation of alpha-fetoprotein in the presence of methylene blue resulted in the loss of the copper(II)-binding ability of the protein in parallel with the destruction of the histidyl residues. A synthetic amino-terminal undecapeptide of alpha-fetoprotein also bound copper(II) ion. These results indicate that the histidyl residue at the amino-terminal region of alpha-fetoprotein plays an important role in the copper(II)-binding ability of the protein.

Carcinoma, Hepatocellular↗
PubMed1977

Comparative chemical structures of human alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma.

Human alpha-fetoproteins were purified from umbilical cord serum and from ascites fluid of a patient with hepatoma by affinity chromatography, and their chemical compositions and terminal sequences were compared. The amino acid compositions of these alpha-fetoproteins were similar and in good agreement with the values reported by other investigators. The COOH-terminal 5-amino acid sequence determined by carboxypeptidase digestion and the NH2-terminal 20-amino acid sequence determined by an automated sequence analyzer revealed that both alpha-fetoproteins had the same terminal sequences of amino acids. The sequence analysis showed that a part of each of the proteins lacked its NH2-terminal residues for one or three amino acids. A small difference in the carbohydrate composition of each alpha-fetoprotein was observed. It was concluded that alpha-fetoproteins from fetal serum and from ascites fluid of a patient with hepatoma had very similar structures.

Amino Acid Sequence↗