The Experts below are selected from a list of 99 Experts worldwide ranked by ideXlab platform

Takuo Nakano - One of the best experts on this subject based on the ideXlab platform.

  • Cellulose Acetate Electrophoresis of whey proteins and glycomacropeptide
    Milchwissenschaft-milk Science International, 2009
    Co-Authors: Takuo Nakano, T Watanabe, N Ikawa, E Silvahernandez, L Ozimek
    Abstract:

    Cellulose Acetate Electrophoresis was used to compare electrophoretic patterns of whey components between the two different systems with 0.1 M potassium phosphate buffer, pH 7.0 and 0.1 M pyridine/1.2 M acetic acid buffer, pH 3.5. With potassium phosphate buffer, clear separation was seen among the major proteins, β-lactoglobulin, α-lactalbumin and immunoglobulin. However, the difference of electrophoretic mobility between serum albumin and β-lactoglobulin or between immunoglobulin and lactoferrin was small. The mobility of glycomacropeptide (GMP), a κ-casein derived sialylated glycopeptide, was similar to the mobility of β-lactoglobulin or serum albumin. With pyridine/ acetic acid buffer, all whey proteins showed no positive mobilities, while sialylated glycomacropeptide had a highly positive mobility. Differences in electrophoretic profiles were also found between sweet whey and acid whey, and between sweet whey prepared from fresh milk and commercial sweet whey. Results of amino acid analysis indicated that GMP fraction with a trace (<1 mol %) of tyrosine, phenylalanine, histidine and arginine (amino acids absent in GMP) can be obtained by Electrophoresis in pyridine/ acetic acid. The method with pyridine/acetic acid can be used for detection of GMP in whey added margarine as well as purification of a small amount of GMP from sweet whey.

  • a simple rapid method to estimate hyaluronic acid concentrations in rooster comb and wattle using Cellulose Acetate Electrophoresis
    Journal of Agricultural and Food Chemistry, 1994
    Co-Authors: Takuo Nakano, Kayo Nakano, J S Sim
    Abstract:

    A simple rapid method of quantitative analysis of hyaluronic acid (HA) from comb and wattle tissues is described. The technique involves short-time acetone drying and proteolysis of tissues, Cellulose Acetate Electrophoresis of the digests without deproteinization, and measurement of absorbance of the solution of Alcian Blue extracted from the HA band. With this method, the determination of HA, which may take 1 week or longer with other methods, could be made within a day.

J S Sim - One of the best experts on this subject based on the ideXlab platform.

Norbert Blanckaert - One of the best experts on this subject based on the ideXlab platform.

  • Detection and classification of paraproteins by capillary immunofixation/subtraction.
    Clinical Chemistry, 1998
    Co-Authors: Xavier Bossuyt, Ann Bogaerts, Gilberte Schiettekatte, Norbert Blanckaert
    Abstract:

    A selection of 58 specimens with a monoclonal component identified by immunoElectrophoresis and/or immunofixation was analyzed with the immunosubtraction procedure on the Paragon 2000 capillary Electrophoresis system. The capillary system detected 93% of the paraproteins and, using immunosubtraction, correctly identified 91% of the paraproteins. Paraproteins that were detected by immunofixation and/or immunoElectrophoresis but not by capillary Electrophoresis were also missed by agarose Electrophoresis and Cellulose Acetate Electrophoresis. Cellulose Acetate Electrophoresis was the least sensitive method for detection of paraproteins. Only 74% of the monoclonal components were detected by this technique, whereas 86% were revealed by agarose Electrophoresis. In addition to monoclonal paraproteins, we also studied biclonal paraproteins and oligoclonal banding. Capillary Electrophoresis and immunosubtraction correctly detected and identified three specimens containing biclonal paraproteins. In one specimen, capillary zone Electrophoresis detected only one band, whereas agarose gel Electrophoresis detected two bands. The sensitivity for detection and identification of oligoclonal banding by capillary Electrophoresis was inferior to immunofixation.

  • Serum protein Electrophoresis and immunofixation by a semiautomated Electrophoresis system
    Clinical chemistry, 1998
    Co-Authors: Xavier Bossuyt, Ann Bogaerts, Gilberte Schiettekatte, Norbert Blanckaert
    Abstract:

    Semiautomated agarose Electrophoresis and immunofixation performed with Hydrasys-Hyrys (Sebia) were compared with conventional, manually performed methods, including Cellulose Acetate Electrophoresis, immunoElectrophoresis, and immunofixation. Reference intervals for agarose Electrophoresis with Hydrasys-Hyrys were determined. Within-run imprecision (CV) for fraction quantitation with the semiautomated system was between 1% (albumin) and 4.5% (beta-globulin). Total imprecision (CV) was between 2.7% (albumin) and 7.3% (beta-globulin). Semiautomated agarose Electrophoresis showed linear correlation with Cellulose Acetate Electrophoresis. Thirty-four specimens with monoclonal components were analyzed by manual immunoElectrophoresis and immunofixation and by Hydrasys. In one case, a light-chain disease was missed with Hydrasys when the sample was diluted 1:3 (the routine dilution) but not when the sample was assayed undiluted. In another case, the Hydrasys system revealed a small IgGA monoclonal component in addition to the IgA monoclonal component detected by the manual methods. In the other cases, no differences between the manual methods and the semiautomated method were seen with respect to paraprotein identification.

Yasuyuki Okamoto - One of the best experts on this subject based on the ideXlab platform.

  • γ Heavy chain disease screening showing a discrepancy between electrophoretic and nephelometric determinations of serum γ globulin concentration
    Annals of Clinical Biochemistry, 2002
    Co-Authors: Tsunenori Takatani, Keiko Morita, Naomi Takaoka, Masatsuga Tatsumi, Yorio Okuno, Takayuki Masutani, Koichi Murakawa, Akihiro Fukui, Nobuhiko Tsukaguchi, Yasuyuki Okamoto
    Abstract:

    A 75-year-old woman with rheumatoid arthritis showed a discrepancy between the reduced level of serum gamma globulin on Cellulose Acetate Electrophoresis and the normal level of serum IgG determined by laser nephelometry. Although no M-peak was detectable on Cellulose Acetate Electrophoresis, immunoElectrophoresis of the patient's serum revealed a monoclonal protein reacting with anti-IgG antiserum but not with anti-kappa or anti-lambda light chain antiserum. Western blotting of the patient's serum showed abnormal low-molecular-weight gamma chains. Thus, the patient was diagnosed with gamma heavy chain disease. A comparison of gamma globulin levels determined by different methods may be useful when screening for this disease.

  • Gamma heavy chain disease screening showing a discrepancy between electrophoretic and nephelometric determinations of serum gamma globulin concentration.
    Annals of clinical biochemistry, 2002
    Co-Authors: Tsunenori Takatani, Keiko Morita, Naomi Takaoka, Masatsuga Tatsumi, Yorio Okuno, Takayuki Masutani, Koichi Murakawa, Akihiro Fukui, Nobuhiko Tsukaguchi, Yasuyuki Okamoto
    Abstract:

    A 75-year-old woman with rheumatoid arthritis showed a discrepancy between the reduced level of serum gamma globulin on Cellulose Acetate Electrophoresis and the normal level of serum IgG determined by laser nephelometry. Although no M-peak was detectable on Cellulose Acetate Electrophoresis, immunoElectrophoresis of the patient's serum revealed a monoclonal protein reacting with anti-IgG antiserum but not with anti-kappa or anti-lambda light chain antiserum. Western blotting of the patient's serum showed abnormal low-molecular-weight gamma chains. Thus, the patient was diagnosed with gamma heavy chain disease. A comparison of gamma globulin levels determined by different methods may be useful when screening for this disease.

Elice M. Brooks - One of the best experts on this subject based on the ideXlab platform.

  • Prevalence and Properties of the IntestinalAlkaline Phosphatase Identified in Serum by Cellulose Acetate Electrophoresis
    2015
    Co-Authors: Williams C. Griffiths, Paul D. Camara, Mark Rosner, Robert Lev, Elice M. Brooks
    Abstract:

    We investigatedthe prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identi-fied in human serum by Cellulose Acetate Electrophoresis in 8 % of fasting serum samples from hospital patients (n = 500) and in 35 % of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated be-tween types 1 and 2). The intestinal ALP electrophoretic band was usually heterogeneous and contained two major subtypesof ALP. Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct re-gions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa. An-odic intestinal ALP was resistant to treatment with levami-sole and neuraminidase and comigrated with ALP fro

  • Prevalence and properties of the intestinal alkaline phosphatase identified in serum by Cellulose Acetate Electrophoresis.
    Clinical chemistry, 1992
    Co-Authors: Williams C. Griffiths, Mark Rosner, Robert Lev, Paul Camara, Elice M. Brooks
    Abstract:

    We investigated the prevalence and characteristics of intestinal alkaline phosphatase (ALP; EC 3.1.3.1) identified in human serum by Cellulose Acetate Electrophoresis in 8% of fasting serum samples from hospital patients (n = 500) and in 35% of fasting serum samples from patients with diabetes mellitus (n = 106; not differentiated between types 1 and 2). The intestinal ALP electrophoretic band was usually heterogeneous and contained two major subtypes of ALP. Isoelectric focusing of intestinal-ALP-positive serum treated with levamisole and neuraminidase (EC 3.2.1.18) revealed two distinct regions of enzymatic activity that comigrated with ALP extracted from small intestinal and colonic mucosa. Anodic intestinal ALP was resistant to treatment with levamisole and neuraminidase and comigrated with ALP from small intestinal mucosa. The more-cathodic intestinal ALP, which comigrated with ALP from colonic mucosa, was completely inhibited by levamisole and converted by neuraminidase to a species with a more basic pI than that of neuraminidase-digested tissue-nonspecific form. This component of intestinal ALP may be of vascular origin.