Electrophoretic and Immunological Characterization of Acidic and Neutral Amylo-1,4-Glucosidase (Acid Maltase) in Human Tissues and Evidence for Two Variants in Acid Maltase Deficiency

RNAases (ribonucleases), purified from four human tissues, as well as bovine pancreatic RNAase (RNAase A), were studied by immunodiffusion methods and by two different primary binding tests. The enzymes fell into two groups immunologically, those purified from plasma and pancreas in one and those from spleen and liver in the other. No antigenic cross-reaction between the two groups was detected by any of the immunoassays used. There was a slight antigenic cross-reaction between the human and bovine pancreatic RNAases. The liver and spleen RNAases were immunologically identical by all criteria used, whereas a small but consistent antigenic difference between the human plasma and human pancreas enzymes was detected. The significance of this difference between the human plasma and pancreas RNAases is discussed in relation to similarities and differences in their properties.

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Biochemical and immunological characterization of alpha-amylase isoenzymes of Araucaria araucana

Physiologia Plantarum ◽

10.1034/j.1399-3054.1994.920120.x ◽

1994 ◽

Vol 92 (1) ◽

pp. 149-159

Author(s):

Elba Acevedo ◽

Liliana Cardemil

Keyword(s):

Alpha Amylase ◽

Immunological Characterization ◽

Araucaria Araucana ◽

Amylase Isoenzymes

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Characterization of the lipid droplet-associated protein MLDP in human tissues and in hepatocyte steatosis

Zeitschrift für Gastroenterologie ◽

10.1055/s-0029-1246408 ◽

2010 ◽

Vol 48 (01) ◽

Author(s):

M Hashani ◽

M koenig ◽

LM Pawella ◽

P Schirmacher ◽

BK Straub

Keyword(s):

Lipid Droplet ◽

Human Tissues ◽

Hepatocyte Steatosis

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The Immunological Characterization of Human Antibodies to Factor VIII Isolated by Immuno-Affinity Chromatography

Thrombosis and Haemostasis ◽

10.1055/s-0038-1650129 ◽

1981 ◽

Vol 45 (01) ◽

pp. 060-064 ◽

Cited By ~ 10

Author(s):

M L Kavanagh ◽

C N Wood ◽

J F Davidson

Keyword(s):

Factor Viii ◽

Affinity Chromatography ◽

Gel Filtration ◽

Immunological Characterization ◽

Human Antibodies ◽

Heavy Chains ◽

Light Chain Type ◽

Antibody Preparations ◽

Chain Type

SummaryNine human antibodies to factor VIII were isolated from haemophilic plasmas by affinity chromatography and gel filtration and six were subsequently subjected to immunological characterization. Three partially purified preparations were similarly characterized. Eight of the antibodies were characterized as being exclusively IgG and one preparation was found to contain IgM. Seven of the antibodies contained only a single light chain type, four being of type lambda and three of type kappa. Two antibody preparations contained both kappa and lambda light chains. In four of the preparations, only a single heavy chain sub-class could be demonstrated, three of IgG3 and one of IgG4. Of the remainder, three were a mixture of IgG3 and IgG4 sub-classes and one contained both IgG2 and IgG4. IgG sub-classification could not be achieved with the IgM-containing preparation. These results demonstrate a restricted heterogeneity of light and heavy chains in human antibodies to factor VIII.

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