Primary structure of hemocyanin from Palinurus vulgaris

Panulirus Interruptus Hemocyanin:The amino-acid sequence of the region containing one copper-binding site and the sites susceptible to limited proteolysis

Vereijken, Johan M.
de Vlieg, Jacob
Beintema, Jaap J.

January 1984

The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three...

Structural and functional heterogeneity of hemocyanin: intra- and inter-specific comparison in four species of portunid crabs (Crustacea : Portunidae)

GIOMI, FOLCO
DI MURO, PAOLO
BELTRAMINI, MARIANO
RAICEVICH S
FERRARESE A
PRANOVI F

January 2007

This work is focused on hemocyanin (Hc) heterogeneity at population level and on the biochemical cha...

Panulirus Interruptus Hemocyanin: The amino-acid sequence of the region containing one copper-binding site and the sites susceptible to limited proteolysis

Vereijken, Johan M.
de Vlieg, Jacob
Beintema, Jaap J.

January 1984

The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three...

Primary structure of hemocyanin from Palinurus vulgaris

Jekel, PA
Neuteboom, B
Beintema, JJ

October 1996

The primary structure of hemocyanin from the spiny lobster Palinurus vulgaris was determined using a...

Partial amino acid sequence of a hemocyanin subunit from Palinurus vulgaris

Neuteboom, B
Dokter, W
van Gijsen, Jan
Rensink, Herman
de Vries, J
Beintema, J.J

January 1989

1. Hemocyanin from the spiny lobster Palinurus vulgaris was separated into two fractions, which were...

PRIMARY STRUCTURE OF HEMOCYANIN SUBUNIT-C FROM PANULIRUS-INTERRUPTUS

NEUTEBOOM, B
JEKEL, PA
BEINTEMA, JJ

May 1992

The amino acid sequence of the hemocyanin subunit c from the spiny lobster, Panulirus interruptus, h...

Quaternary structure of the European spiny lobster (Palinurus elephas) 1 x 6-mer hemocyanin from cryoEM and amino acid sequence data

Meissner, U.
Stohr, M.
Kusche, K.
Burmester, T.
Stark, H.
Harris, J. R.
Orlova, E. V.
Markl, J.

January 2003

Arthropod hemocyanins are large respiratory proteins that are composed of up to 48 subunits (8 x 6-m...

Structure of arthropod hemocyanin

Bak, Henk J.
Neuteboom, Ben
Jekel, Peter A.
Soeter, Nell M.
Vereijken, Johan M.
Beintema, Jaap J.

August 1986

AbstractHemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods...

Structure of arthropod hemocyanin

Bak, H. J.
Neuteboom, B.
Jekel, P. A.
Soeter, N. M.
Vereijken, J. M.
Beintema, J. J.

August 1986

Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and mol...

The structure of arthropod hemocyanins

Linzen, B.
Soeter, N. M.
Riggs, A. F.
Schneider, H. J.
Schartau, W.
Moore, M. D.
Yokota, E.
Behrens, P. Q.
Nakashima, H.
Takagi, T.
Nemoto, T.
Vereijken, J. M.
Bak, H. J.
Beintema, J. J.
Volbeda, A.
Gaykema, W. P. J.
Hol, W. G. J.

January 1985

Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and mol...

Primary structure of the acidic carbohydrate chain of hemocyanin from Panulirus interruptus

van Kuik, J.A.
Breg, J.
Kolsteeg, C.E.M.
Kamerling, J.P.
Vliegenthart, J.F.G.

August 1987

AbstractThe N-glycosidic carbohydrate chains of hemocyanin from the spiny lobster Panulirus interrup...

HEXAMERS OF SUBUNIT-II FROM LIMULUS HEMOCYANIN (A 48-MER) HAVE THE SAME QUATERNARY STRUCTURE AS WHOLE PANULIRUS HEMOCYANIN MOLECULES

MAGNUS, KA
LATTMAN, EE
VOLBEDA, A
HOL, WGJ

January 1991

Hemocyanins are copper-containing proteins that transport oxygen in a variety of invertebrates. Cons...

Hemocyanin from Palinurus elephas: general properties and effects of heavy metals

Andrea Bellelli
Lello Zolla
Bruno Giardina
Sergio Costantini
Angelo Cau
Maurizio Brunori

January 1985

The structural and functional properties of hemocyanin from the lobster Palinurus elephas indicate t...

Panulirus Interruptus Hemocyanin:The amino-acid sequence of the region containing one copper-binding site and the sites susceptible to limited proteolysis

Vereijken, Johan M.
de Vlieg, Jacob
Beintema, Jaap J.

January 1984

The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three...

Structural and functional heterogeneity of hemocyanin: intra- and inter-specific comparison in four species of portunid crabs (Crustacea : Portunidae)

GIOMI, FOLCO
DI MURO, PAOLO
BELTRAMINI, MARIANO
RAICEVICH S
FERRARESE A
PRANOVI F

January 2007

This work is focused on hemocyanin (Hc) heterogeneity at population level and on the biochemical cha...

Panulirus Interruptus Hemocyanin: The amino-acid sequence of the region containing one copper-binding site and the sites susceptible to limited proteolysis

Vereijken, Johan M.
de Vlieg, Jacob
Beintema, Jaap J.

January 1984

The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three...

Primary structure of hemocyanin from Palinurus vulgaris

Jekel, PA
Neuteboom, B
Beintema, JJ

October 1996

The primary structure of hemocyanin from the spiny lobster Palinurus vulgaris was determined using a...

Partial amino acid sequence of a hemocyanin subunit from Palinurus vulgaris

Neuteboom, B
Dokter, W
van Gijsen, Jan
Rensink, Herman
de Vries, J
Beintema, J.J

January 1989

1. Hemocyanin from the spiny lobster Palinurus vulgaris was separated into two fractions, which were...

PRIMARY STRUCTURE OF HEMOCYANIN SUBUNIT-C FROM PANULIRUS-INTERRUPTUS

NEUTEBOOM, B
JEKEL, PA
BEINTEMA, JJ

May 1992

The amino acid sequence of the hemocyanin subunit c from the spiny lobster, Panulirus interruptus, h...

Quaternary structure of the European spiny lobster (Palinurus elephas) 1 x 6-mer hemocyanin from cryoEM and amino acid sequence data

Meissner, U.
Stohr, M.
Kusche, K.
Burmester, T.
Stark, H.
Harris, J. R.
Orlova, E. V.
Markl, J.

January 2003

Arthropod hemocyanins are large respiratory proteins that are composed of up to 48 subunits (8 x 6-m...

Structure of arthropod hemocyanin

Bak, Henk J.
Neuteboom, Ben
Jekel, Peter A.
Soeter, Nell M.
Vereijken, Johan M.
Beintema, Jaap J.

August 1986

AbstractHemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods...

Structure of arthropod hemocyanin

Bak, H. J.
Neuteboom, B.
Jekel, P. A.
Soeter, N. M.
Vereijken, J. M.
Beintema, J. J.

August 1986

Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and mol...

The structure of arthropod hemocyanins

Linzen, B.
Soeter, N. M.
Riggs, A. F.
Schneider, H. J.
Schartau, W.
Moore, M. D.
Yokota, E.
Behrens, P. Q.
Nakashima, H.
Takagi, T.
Nemoto, T.
Vereijken, J. M.
Bak, H. J.
Beintema, J. J.
Volbeda, A.
Gaykema, W. P. J.
Hol, W. G. J.

January 1985

Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and mol...

Primary structure of the acidic carbohydrate chain of hemocyanin from Panulirus interruptus

van Kuik, J.A.
Breg, J.
Kolsteeg, C.E.M.
Kamerling, J.P.
Vliegenthart, J.F.G.

August 1987

AbstractThe N-glycosidic carbohydrate chains of hemocyanin from the spiny lobster Panulirus interrup...

HEXAMERS OF SUBUNIT-II FROM LIMULUS HEMOCYANIN (A 48-MER) HAVE THE SAME QUATERNARY STRUCTURE AS WHOLE PANULIRUS HEMOCYANIN MOLECULES

MAGNUS, KA
LATTMAN, EE
VOLBEDA, A
HOL, WGJ

January 1991

Hemocyanins are copper-containing proteins that transport oxygen in a variety of invertebrates. Cons...

Hemocyanin from Palinurus elephas: general properties and effects of heavy metals

Andrea Bellelli
Lello Zolla
Bruno Giardina
Sergio Costantini
Angelo Cau
Maurizio Brunori

January 1985

The structural and functional properties of hemocyanin from the lobster Palinurus elephas indicate t...

Panulirus Interruptus Hemocyanin:The amino-acid sequence of the region containing one copper-binding site and the sites susceptible to limited proteolysis

Vereijken, Johan M.
de Vlieg, Jacob
Beintema, Jaap J.

January 1984

The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three...

Structural and functional heterogeneity of hemocyanin: intra- and inter-specific comparison in four species of portunid crabs (Crustacea : Portunidae)

GIOMI, FOLCO
DI MURO, PAOLO
BELTRAMINI, MARIANO
RAICEVICH S
FERRARESE A
PRANOVI F

January 2007

This work is focused on hemocyanin (Hc) heterogeneity at population level and on the biochemical cha...

Panulirus Interruptus Hemocyanin: The amino-acid sequence of the region containing one copper-binding site and the sites susceptible to limited proteolysis

Vereijken, Johan M.
de Vlieg, Jacob
Beintema, Jaap J.

January 1984

The amino-acid sequence of a part of Panulirus interruptus hemocyanin subunit a comprising the three...

Primary structure of hemocyanin from Palinurus vulgaris

Abstract

Extracted data

Primary structure of hemocyanin from Palinurus vulgaris

Abstract

Extracted data

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