The soluble form of rat liver alpha-mannosidase is immunologically related to the endoplasmic reticulum membrane alpha-mannosidase.

This publication has 28 references indexed in Scilit:

• Attachment of terminal N-acetylglucosamine to asparagine-linked oligosaccharides occurs in central cisternae of the golgi stack
  Cell, 1985
• Glucosidase II, a glycoprotein of the endoplasmic reticulum membrane. Proteolytic cleavage into enzymically active fragments
  Biochemistry, 1985
• The effect of 1-deoxymannojirimycin on rat liver α-mannosidases
  Biochemical and Biophysical Research Communications, 1984
• Purification by affinity chromatography of glucosidase I, an endoplasmic reticulum hydrolase involved in the processing of asparagine‐linked oligosaccharides
  European Journal of Biochemistry, 1984
• Isolation of a homogeneous glucosidase II from pig kidney microsomes
  European Journal of Biochemistry, 1984
• Separation of neutral oligosaccharides by high-performance liquid chromatography
  Analytical Biochemistry, 1981
• Ultrasensitive Stain for Proteins in Polyacrylamide Gels Shows Regional Variation in Cerebrospinal Fluid Proteins
  Science, 1981
• Evidence for a non-lysosomal α-mannosidase in rat liver homogenates
  Biochimica et Biophysica Acta (BBA) - Enzymology, 1971
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970
• DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*
  Annals of the New York Academy of Sciences, 1964