Glycosylation of annexin I and annexin II.
Human placental annexin I and annexin II were shown to be glycosylated by one-dimensional affinity blotting with the lectin concanavalin A, which recognizes D-mannose and D-glucose residues. Further evidence that annexin I and annexin II are glycosylated was provided by the finding that these proteins incorporated D-[2,6-3H]mannose and D-[6-3H]glucose when they were biosynthesized by the human squamous carcinoma cell line SqCC/Y1. Annexin I and annexin II could be rapidly purified from a human placental membrane extract by concanavalin A-Sepharose, which indicated that these proteins contain two biantennary mannosyl residues.
Goulet
F
F
Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510.
Moore
K G
KG
Sartorelli
A C
AC
D017305:Annexin A1 / Q000096:biosynthesis* / Q000302:isolation & purification; D017306:Annexin A2 / Q000096:biosynthesis* / Q000302:isolation & purification; D002294:Carcinoma, Squamous Cell; D002462:Cell Membrane / Q000737:chemistry; D002846:Chromatography, Affinity; D005260:Female; D005947:Glucose / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D010920:Placenta / Q000737:chemistry; D011247:Pregnancy; D014407:Tumor Cells, Cultured
D017305:Annexin A1; D017306:Annexin A2; D008715:Methionine; D005947:Glucose; D008358:Mannose