Kunihiko Kobayashi

ORCID: 0000-0003-4319-7512
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Research Areas
  • Proteins in Food Systems
  • Microencapsulation and Drying Processes
  • Monoclonal and Polyclonal Antibodies Research
  • Glycosylation and Glycoproteins Research
  • Protein purification and stability
  • Diabetes, Cardiovascular Risks, and Lipoproteins
  • Protein Hydrolysis and Bioactive Peptides
  • Lung Cancer Diagnosis and Treatment
  • Enzyme Production and Characterization
  • Neonatal Respiratory Health Research
  • Pickering emulsions and particle stabilization
  • Lipoproteins and Cardiovascular Health
  • Pleural and Pulmonary Diseases
  • Food Chemistry and Fat Analysis
  • Lung Cancer Treatments and Mutations
  • Food composition and properties
  • Peroxisome Proliferator-Activated Receptors
  • Neuroscience of respiration and sleep
  • Respiratory viral infections research
  • Biochemical effects in animals
  • Pregnancy and preeclampsia studies
  • Blood disorders and treatments
  • Blood groups and transfusion
  • Celiac Disease Research and Management
  • Cancer, Lipids, and Metabolism

Saitama Medical University
2009-2025

Sapporo Hokuyu Hospital
2008-2021

Saitama International Medical Center
2013-2017

Saitama University
2014

Hokkaido University
1997-2009

Yokohama City University
2009

Nippon Medical School
1990-2009

Hokkaido University Hospital
2008

Saitama Cancer Center
1993-2003

Pediatrics and Genetics
2002

This multicenter phase II study was undertaken to investigate the efficacy and feasibility of gefitinib for patients with advanced non-small-cell lung cancer (NSCLC) harboring epidermal growth factor receptor (EGFR) mutations without indication chemotherapy as a result poor performance status (PS).Chemotherapy-naïve PS (patients 20 74 years age Eastern Cooperative Oncology Group 3 4, 75 79 2 >or= 80 1 4) who had EGFR examined by peptide nucleic acid-locked acid polymerase chain reaction...

10.1200/jco.2008.18.7658 article EN Journal of Clinical Oncology 2009-02-18

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTImprovement of emulsifying properties egg white proteins by the attachment polysaccharide through Maillard reaction in a dry stateAkio. Kato, Kazuaki. Minaki, and Kunihiko. KobayashiCite this: J. Agric. Food Chem. 1993, 41, 4, 540–543Publication Date (Print):April 1, 1993Publication History Published online1 May 2002Published inissue 1 April 1993https://doi.org/10.1021/jf00028a006Request reuse permissionsArticle Views1376Altmetric-Citations148LEARN...

10.1021/jf00028a006 article EN Journal of Agricultural and Food Chemistry 1993-04-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTNew approach to improve the gelling and surface functional properties of dried egg white by heating in dry stateAkio Kato, Hisham Radwan Ibrahim, Hiroyuki Watanabe, Kazuo Honma, Kunihiko KobayashiCite this: J. Agric. Food Chem. 1989, 37, 2, 433–437Publication Date (Print):March 1, 1989Publication History Published online1 May 2002Published inissue 1 March...

10.1021/jf00086a036 article EN Journal of Agricultural and Food Chemistry 1989-03-01

A new human pneumovirus, provisionally designated metapneumovirus, was discovered by Dutch researchers. We examined 142 serum samples from the general population aged 1 month to 35 years in Japan for metapneumovirus antibody indirect immunofluorescence assays using metapneumovirus-infected monkey kidney cells. The overall prevalence of infection 72.5%. seropositive rate lowest age group 6 months year and gradually increased with age. All children had been exposed 10 years. results show that...

10.1002/jmv.10391 article EN Journal of Medical Virology 2003-04-09

Journal Article Functional Protein–Polysaccharide Conjugate Prepared by Controlled Dry-heating of Ovalbumin–Dextran Mixtures Get access Akio Kato, Kato Department Agricultural Chemistry, Faculty Agriclture, Yamaguchi University, 753, Japan Search for other works this author on: Oxford Academic Google Scholar Youko Sasaki, Sasaki Ritsuko Furuta, Furuta Kunihiko Kobayashi and Biological Volume 54, Issue 1, 1 January 1990, Pages 107–112, https://doi.org/10.1080/00021369.1990.10869907 Published:...

10.1080/00021369.1990.10869907 article EN Agricultural and Biological Chemistry 1990-01-01

ABSTRACT A new method was established to estimate the foaming properties of proteins from conductivity foams using a simple apparatus that consisted glass column with cell. close correlation observed between initial and foam volumes heat‐denatured ovalbumins or 11 native proteins, suggesting can be used as measure power. In addition, obtained stability determined changes in volume time also estimated foams. The advantages measurements are determine more simply accurately than currently methods.

10.1111/j.1365-2621.1983.tb14788.x article EN Journal of Food Science 1983-01-01

Casein was conjugated with dextran and galactomannan in a controlled dry state at relative humidity of 79% 60°C for 24 hr. The covalent attachment polysaccharides to casein confirmed by SDS-PAGE HPLC. emulsifying activity the casein-dextran casein-galactomannan conjugates 1.5 times higher than that casein. emulsion stability 10 improvement these properties reached steady when conjugation polysaccharide done hr state, suggesting rapid formation through Maillard reaction case Compared...

10.1271/bbb.56.567 article EN Bioscience Biotechnology and Biochemistry 1992-01-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructural and gelling properties of dry-heated egg white proteinsAkio Kato, Hisham Radwan Ibrahim, Hiroyuki Watanabe, Kazuo Honma, Kunihiko KobayashiCite this: J. Agric. Food Chem. 1990, 38, 1, 32–37Publication Date (Print):January 1990Publication History Published online1 May 2002Published inissue 1 January 1990https://pubs.acs.org/doi/10.1021/jf00091a007https://doi.org/10.1021/jf00091a007research-articleACS PublicationsRequest reuse...

10.1021/jf00091a007 article EN Journal of Agricultural and Food Chemistry 1990-01-01

Changes in the emulsifying and foaming properties of ovalbumin, 7S globulin, κ-casein, β-lactoglobulin bovine serum albumin were followed during heat denaturation, these surface correlated with corresponding hydrophobicity, order to investigate role hydrophobicity proteins. The globulin κ-casein increased while that decreased. activity emulsion stability proteins linearly although protein structure changed greatly denaturation. On other hand, power curvilinearly No significant correlation...

10.1271/bbb1961.47.33 article EN Agricultural and Biological Chemistry 1983-01-01

ABSTRACT A method was developed to measure the emulsifying activity and emulsion stability of proteins using a simple apparatus consisting glass column with conductivity cell. significant correlation observed between 10 determined by examined in this paper turbidity Pearce Kinsella (1978). These results suggest that properties can be estimated measuring changes emulsion. The advantages are accurately simply proteins, because directly automatically measures physical constant (that is, conductivity)

10.1111/j.1365-2621.1985.tb13276.x article EN Journal of Food Science 1985-01-01

The effects of partial denaturation were investigated on the surface properties ovalbumin and lysozyme. tension proteins decreased greatly as proceeded. emulsifying foaming remarkably improved by heat without coagulation. increased with denaturation, correlated linearly hydrophobicity. On other hand, protein incresed correlating curvilinearly power foam stability SDS-bound did not improve much those heatdenatured ovalbumin, although hydrophobicity to same extent denaturation. relationship...

10.1271/bbb1961.45.2755 article EN Agricultural and Biological Chemistry 1981-01-01

Changes in the emulsifying and foaming properties of ovalbumin, 7S globulin, κ-casein, β-lactoglobuHn bovine serum albumin were followed during heat denaturation, these surface correlated with corresponding hydrophobicity, order to investigate role hydrophobicity proteins. The globulin jc-casein increased while that decreased. activity emulsion stability proteins linearly although protein structure changed greatly denaturation. On other hand, power curvilinearly No significant correlation...

10.1080/00021369.1983.10865579 article EN Agricultural and Biological Chemistry 1983-01-01

Changes to the conformation and functional properties of soy protein caused by mild acid treatment were investigated. When a 2% solution in 0.05 N HCl was heated for 30min at 95°C, protein, including its solubility, emulsifying foaming properties, greatly improved. It found that can be deamidated preferentially without significant cleavage peptide bonds under these carefully controlled conditions dilute (0.05 95°C 30 min). The increased with an increase surface hydrophobicity early stage...

10.1271/bbb1961.49.1251 article EN Agricultural and Biological Chemistry 1985-01-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTImprovement of the functional properties insoluble gluten by pronase digestion followed dextran conjugationAkio Kato, Kazuhiko Shimokawa, and Kunihiko KobayashiCite this: J. Agric. Food Chem. 1991, 39, 6, 1053–1056Publication Date (Print):June 1, 1991Publication History Published online1 May 2002Published inissue 1 June 1991https://pubs.acs.org/doi/10.1021/jf00006a010https://doi.org/10.1021/jf00006a010research-articleACS PublicationsRequest reuse...

10.1021/jf00006a010 article EN Journal of Agricultural and Food Chemistry 1991-06-01

ABSTRACT Complete genes encoding the predicted nucleoprotein (N), phosphoprotein (P), matrix protein (M), fusion (F), M2-1protein, M2-2protein, small hydrophobic (SH), and attachmentprotein (G) of seven newly isolated human metapneumoviruses (hMPVs) were analyzed compared with previously published data for hMPV genes. Phylogenetic analysis nucleotide sequences indicated that there two genetic groups, tentatively named groups 1 2, similar to grouping respiratory syncytial virus. Although...

10.1128/jcm.42.8.3406-3414.2004 article EN Journal of Clinical Microbiology 2004-08-01

The surface properties of deamidated gluten were investigated with respect to their conformational changes. helix content decreased curvilinearly its decrease deamidation. tension in proportion the degree On other hand, hydrophobicity increased remarkably emulsifying improved greatly by deamidation, correlating linearly hydrophobicity. From these results, relationships between changes and functional are discussed.

10.1271/bbb1961.46.1583 article EN Agricultural and Biological Chemistry 1982-01-01

Heat-induced gelation in a mixed system of α-lactalbumin (La) and β-lactoglobulin (Lg) was studied to elucidate the gelling properties whey protein. An Lg concentration 4% (w/v) required for formation self-supporting gel following heating at 80°C 30 min 100 mM potassium phosphate buffer (pH 6.8). Solutions La, even up protein 8% (w/v), did not under same conditions. The addition 6% La 2% caused significant increase hardness, although each individually form these concentrations. By adding Lg,...

10.1271/bbb.56.1697 article EN Bioscience Biotechnology and Biochemistry 1992-01-01
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