A glyco-phosphoprotein in human milk

SummaryA highly glycosylated phosphoprotein (HGPP) was isolated from a human casein fraction by reversed-phase high-performance liquid chromatography. This component contained carbohydrates to ∼ 38·2% (w/w) and phosphorus to ∼ 1·6% (w/w). The molecular weight of this HGPP as estimated by sodium dodecyl sulphate–polyacrylamide gel electrophoresis ∼ 41000. Ultracentrifugal analysis revealed that the sedimentation coefficient of the HGPP was 2·6S in a 10 mM-imidazole-HCl buffer at pH 7·0 and 27 °C, but this component interacted with human κ-casein and formed a complex with s = 10·4S.

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Separation of proteins by consecutive sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and reversed phase high performance liquid chromatography

Biomedical Chromatography ◽

10.1002/bmc.1130050209 ◽

1991 ◽

Vol 5 (2) ◽

pp. 86-89 ◽

Cited By ~ 7

Author(s):

Batia Kaplan ◽

Mordechai Pras

Keyword(s):

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

Sodium Dodecyl Sulfate ◽

Gel Electrophoresis ◽

High Performance ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Reversed Phase ◽

Polyacrylamide Gel ◽

Separation Of Proteins

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Isolation and purification of amyloid protein A by sodium dodecyl sulphate polyacrylamide gel electrophoresis and reversed-phase high-performance liquid chromatography

Journal of Chromatography B Biomedical Sciences and Applications ◽

10.1016/0378-4347(92)80468-6 ◽

1992 ◽

Vol 573 (1) ◽

pp. 17-22 ◽

Cited By ~ 13

Author(s):

Batia Kaplan ◽

Mordechai Pras ◽

Mordchai Ravid

Keyword(s):

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

Gel Electrophoresis ◽

High Performance ◽

Polyacrylamide Gel Electrophoresis ◽

Protein A ◽

Sodium Dodecyl ◽

Reversed Phase ◽

Amyloid Protein ◽

Isolation And Purification

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Breast cancer protein StarD10 identified by three-dimensional separation using free-flow electrophoresis, reversed-phase high-performance liquid chromatography, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis

Electrophoresis ◽

10.1002/elps.200406197 ◽

2005 ◽

Vol 26 (6) ◽

pp. 1029-1037 ◽

Cited By ~ 6

Author(s):

Peter Hoffmann ◽

Monilola A. Olayioye ◽

Robert L. Moritz ◽

Geoffrey J. Lindeman ◽

Jane E. Visvader ◽

...

Keyword(s):

Breast Cancer ◽

High Performance Liquid Chromatography ◽

Liquid Chromatography ◽

Sodium Dodecyl Sulfate ◽

Gel Electrophoresis ◽

High Performance ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Three Dimensional ◽

Reversed Phase

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Heterogeneity of antifreeze polypeptides from the Newfoundland winter flounder, Pseudopleuronectes americanus

Canadian Journal of Zoology ◽

10.1139/z84-006 ◽

1984 ◽

Vol 62 (1) ◽

pp. 28-33 ◽

Cited By ~ 38

Author(s):

Ron M. Fourney ◽

Shashikant B. Joshi ◽

Ming H. Kao ◽

Choy L. Hew

Keyword(s):

Molecular Weight ◽

High Performance Liquid Chromatography ◽

Gel Electrophoresis ◽

High Performance ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Winter Flounder ◽

Pseudopleuronectes Americanus ◽

Reverse Phase ◽

Antifreeze Polypeptides

The heterogeneity of Newfoundland winter flounder antifreeze polypeptides was analyzed by reverse phase high performance liquid chromatography and by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Seven antifreeze polypeptide components could be readily demonstrated. Five of the components were similar in molecular weight (3300) and amino acid composition. Two of the antifreeze polypeptide components were larger (4500) and contained valine. The two major components (components 6 and 8) were identical to those reported earlier from our laboratories.

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