D-Galactose binding lectins from the tunicate Ascidia malaca: Subunit characterization and hemocyte surface distribution

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Abstract

D-galactose specific lectins purified from Ascidia malaca serum contain a major protein component with an apparent molecular weight of about 58,000 daltons, which moves more rapidly under non-reducing conditions. Intramolecular disulfide linkages can explain this behaviour, suggesting a compact protein structure. Membrane lectins have been demonstrated on the surface of about 34% hemocytes by immunofluorescent methods using a rabbit antiserum against the isolated serum lectins. Small, medium and large hemocytes can be positive, as also shown by binding on Sepharose spherules or by rosette formation with sheep and rabbit erythrocytes. Binding is inhibited by the same sugars specific for the serum lectins. Finally, antibodies to the serum lectins specifically agglutinate the hemocytes. This evidence supports the hypothesis that a lectin with the same specificity and certain structural similarities can be found free in the serum and present on hemocyte surfaces. © 1988.
Lingua originaleEnglish
pagine (da-a)495-507
Numero di pagine13
RivistaDevelopmental and Comparative Immunology
Volume12
Stato di pubblicazionePublished - 1988

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Galectins
Hemocytes
Urochordata
Galactose
Lectins
Serum
Rabbits
Rosette Formation
Disulfides
Sepharose
Immune Sera
Sheep
Proteins
Erythrocytes
Molecular Weight
Membranes
Antibodies

All Science Journal Classification (ASJC) codes

  • Immunology
  • Developmental Biology

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title = "D-Galactose binding lectins from the tunicate Ascidia malaca: Subunit characterization and hemocyte surface distribution",
abstract = "D-galactose specific lectins purified from Ascidia malaca serum contain a major protein component with an apparent molecular weight of about 58,000 daltons, which moves more rapidly under non-reducing conditions. Intramolecular disulfide linkages can explain this behaviour, suggesting a compact protein structure. Membrane lectins have been demonstrated on the surface of about 34{\%} hemocytes by immunofluorescent methods using a rabbit antiserum against the isolated serum lectins. Small, medium and large hemocytes can be positive, as also shown by binding on Sepharose spherules or by rosette formation with sheep and rabbit erythrocytes. Binding is inhibited by the same sugars specific for the serum lectins. Finally, antibodies to the serum lectins specifically agglutinate the hemocytes. This evidence supports the hypothesis that a lectin with the same specificity and certain structural similarities can be found free in the serum and present on hemocyte surfaces. {\circledC} 1988.",
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T1 - D-Galactose binding lectins from the tunicate Ascidia malaca: Subunit characterization and hemocyte surface distribution

AU - Parrinello, Nicolo'

AU - Arizza, Vincenzo

PY - 1988

Y1 - 1988

N2 - D-galactose specific lectins purified from Ascidia malaca serum contain a major protein component with an apparent molecular weight of about 58,000 daltons, which moves more rapidly under non-reducing conditions. Intramolecular disulfide linkages can explain this behaviour, suggesting a compact protein structure. Membrane lectins have been demonstrated on the surface of about 34% hemocytes by immunofluorescent methods using a rabbit antiserum against the isolated serum lectins. Small, medium and large hemocytes can be positive, as also shown by binding on Sepharose spherules or by rosette formation with sheep and rabbit erythrocytes. Binding is inhibited by the same sugars specific for the serum lectins. Finally, antibodies to the serum lectins specifically agglutinate the hemocytes. This evidence supports the hypothesis that a lectin with the same specificity and certain structural similarities can be found free in the serum and present on hemocyte surfaces. © 1988.

AB - D-galactose specific lectins purified from Ascidia malaca serum contain a major protein component with an apparent molecular weight of about 58,000 daltons, which moves more rapidly under non-reducing conditions. Intramolecular disulfide linkages can explain this behaviour, suggesting a compact protein structure. Membrane lectins have been demonstrated on the surface of about 34% hemocytes by immunofluorescent methods using a rabbit antiserum against the isolated serum lectins. Small, medium and large hemocytes can be positive, as also shown by binding on Sepharose spherules or by rosette formation with sheep and rabbit erythrocytes. Binding is inhibited by the same sugars specific for the serum lectins. Finally, antibodies to the serum lectins specifically agglutinate the hemocytes. This evidence supports the hypothesis that a lectin with the same specificity and certain structural similarities can be found free in the serum and present on hemocyte surfaces. © 1988.

UR - http://hdl.handle.net/10447/146460

M3 - Article

VL - 12

SP - 495

EP - 507

JO - Developmental and Comparative Immunology

JF - Developmental and Comparative Immunology

SN - 0145-305X

ER -