Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin

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Standard

Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin. / Engvall, E; Krusius, T; Wewer, U; Ruoslahti, E.

I: Archives of Biochemistry and Biophysics, Bind 222, Nr. 2, 15.04.1983, s. 649-56.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Engvall, E, Krusius, T, Wewer, U & Ruoslahti, E 1983, 'Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin', Archives of Biochemistry and Biophysics, bind 222, nr. 2, s. 649-56.

APA

Engvall, E., Krusius, T., Wewer, U., & Ruoslahti, E. (1983). Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin. Archives of Biochemistry and Biophysics, 222(2), 649-56.

Vancouver

Engvall E, Krusius T, Wewer U, Ruoslahti E. Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin. Archives of Biochemistry and Biophysics. 1983 apr. 15;222(2):649-56.

Author

Engvall, E ; Krusius, T ; Wewer, U ; Ruoslahti, E. / Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin. I: Archives of Biochemistry and Biophysics. 1983 ; Bind 222, Nr. 2. s. 649-56.

Bibtex

@article{402bb8f4ce344057b98aae058b7901fe,
title = "Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin",
abstract = "Laminin was isolated from a rat yolk sac tumor by salt extraction, gel filtration, and affinity chromatography on heparin-Sepharose. The purified laminin gave two polypeptide chains with approximate Mr of 200,000 and 400,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its amino acid composition and electron microscopic appearance were similar to those reported earlier for mouse laminin. Carbohydrate analysis revealed 13% carbohydrate consisting of N-acetylglucosamine, galactose, mannose, fucose, sialic acid, and small amounts of N-acetyl galactosamine. The purified rat laminin was immunologically very similar to mouse laminin as recognized by rabbit antibodies but was antigenically distinct when recognized by mouse antibodies.",
keywords = "Amino Acids, Animals, Antibodies, Carbohydrates, Chemical Phenomena, Chemistry, Glycoproteins, Laminin, Membrane Proteins, Mesonephroma, Mice, Microscopy, Electron, Neoplasm Proteins, Neoplasms, Experimental, Rats, Species Specificity",
author = "E Engvall and T Krusius and U Wewer and E Ruoslahti",
year = "1983",
month = apr,
day = "15",
language = "English",
volume = "222",
pages = "649--56",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press",
number = "2",

}

RIS

TY - JOUR

T1 - Laminin from rat yolk sac tumor: isolation, partial characterization, and comparison with mouse laminin

AU - Engvall, E

AU - Krusius, T

AU - Wewer, U

AU - Ruoslahti, E

PY - 1983/4/15

Y1 - 1983/4/15

N2 - Laminin was isolated from a rat yolk sac tumor by salt extraction, gel filtration, and affinity chromatography on heparin-Sepharose. The purified laminin gave two polypeptide chains with approximate Mr of 200,000 and 400,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its amino acid composition and electron microscopic appearance were similar to those reported earlier for mouse laminin. Carbohydrate analysis revealed 13% carbohydrate consisting of N-acetylglucosamine, galactose, mannose, fucose, sialic acid, and small amounts of N-acetyl galactosamine. The purified rat laminin was immunologically very similar to mouse laminin as recognized by rabbit antibodies but was antigenically distinct when recognized by mouse antibodies.

AB - Laminin was isolated from a rat yolk sac tumor by salt extraction, gel filtration, and affinity chromatography on heparin-Sepharose. The purified laminin gave two polypeptide chains with approximate Mr of 200,000 and 400,000 in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its amino acid composition and electron microscopic appearance were similar to those reported earlier for mouse laminin. Carbohydrate analysis revealed 13% carbohydrate consisting of N-acetylglucosamine, galactose, mannose, fucose, sialic acid, and small amounts of N-acetyl galactosamine. The purified rat laminin was immunologically very similar to mouse laminin as recognized by rabbit antibodies but was antigenically distinct when recognized by mouse antibodies.

KW - Amino Acids

KW - Animals

KW - Antibodies

KW - Carbohydrates

KW - Chemical Phenomena

KW - Chemistry

KW - Glycoproteins

KW - Laminin

KW - Membrane Proteins

KW - Mesonephroma

KW - Mice

KW - Microscopy, Electron

KW - Neoplasm Proteins

KW - Neoplasms, Experimental

KW - Rats

KW - Species Specificity

M3 - Journal article

C2 - 6847209

VL - 222

SP - 649

EP - 656

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -

ID: 34330412