Biomedical Engineering Reference
In-Depth Information
DolPP
Dolichol pyrophosphate
Endo F/H/D
Endopeptidase F/H/D
EPO
Erythropoietin
ER
Endoplasmic reticulum
FT
Fucosyl transferase
Fuc
Fucose
FSH
Follicular stimulating hormone
a
-Glucosidase
Glc Glucose
Gal Galactose
Gnc (GlcNAc)
N
-acetylglucosamine
Glyc T
G
a
Glycosyl transferases
Gn T
N
-acetylglucosaminyl transferase
Gal T
Galactosyl transferases
GalNAc
N
-acetylgalactosamine
GalNAc T
N
-acetylgalactosaminyl transferase
GPI
Glucosylphosphatidylinositol
IFN
g
Interferon
g
IgG
Immunoglobulin G
LH
Luteinizing hormone
Man
Mannose
a
M
a
-Mannosidase
PCR
Polymerase chain reaction
PNGases
Peptide
N
-glycanases
SA
Sialic acid
ST
Sialyl transferase
TSH
Thyroid stimulating hormone
tPA
Tissue plasminogen activator
UDP
Uridine diphosphate
Xyl
Xylose
1
Introduction
To obtain their final structural features and functions, newly formed poly-
peptides undergo various types of modifications, such as folding, conformation
stabilization by disulfide bridges, assembly into homo- or hetero-oligomers,
acquisition of prosthetic groups, specific proteolytic cleavage and covalent
attachment of phosphate, sulfate, fatty acid, complex lipid or sugar groups [1].
The types of modification shown by an individual protein depend on its amino
acid sequence, conformation, as well as on cell type and tissue context [2].
Glycoproteins are a conjugated form of proteins containing one or more
heterosaccharides covalently bound to the polypeptide chain. These are present
in virtually all forms of life and in cell secretions, serum and other body fluids,
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