Glossary for NanoBiotechnology

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glial cells:
Supporting cells of the nervous system, including oligodendrocytes and astrocytes in the vertebrate central nervous system and Schwann cells in the peripheral nervous system.

globular protein:
Any protein with an approximately rounded shape; contrasts with highly elongated, fibrous proteins such as collagen.

glucose:
Six-carbon sugar that plays a major role in the metabolism of living cells. Stored in polymeric form as glycogen in animal cells and as starch in plant cells.

glutaraldehyde:
Small reactive molecule with two aldehyde groups that is often used as a cross-linking fixative.

glycerol:
Small organic molecule that is the parent compound of many small molecules in the cell, including phospholipids.

glycocalyx (cell coat):
Carbohydrate-rich layer that forms the outer coat of a eucaryotic cell. Composed of the oligosaccharides linked to intrinsic plasma membrane glycoproteins and glycolipids, as well as glycoproteins and proteoglycans that have been secreted and reabsorbed onto the cell surface.

glycogen:
Polysaccharide composed exclusively of glucose units used to store energy in animal cells. Large granules of glycogen are especially abundant in liver and muscle cells.

glycolipid:
Membrane lipid molecule with a short carbohydrate chain attached to a hydrophobic tail.

glycolysis:
Ubiquitous metabolic pathway in the cytosol in which sugars are incompletely degraded with production of ATP. (Literally, "sugar splitting.")

glycoprotein:
Any protein with one or more covalently linked oligosaccharide chains. Includes most secreted proteins and most proteins exposed on the outer surface of the plasma membrane.

glycosaminoglycan:
see GAG

Golgi apparatus:
Membrane-bounded organelle in eucaryotic cells where the proteins and lipids made in the endoplasmic reticulum are modified and sorted.

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Parts of the glossary are from the following book:
Copyright 1983, 1989, 1994 From "Molecular Biology of the Cell" by Bruce Alberts, Dennis Bray, Julian Lewis, Martin Raff, Keith Roberts, James D. Watson. Reproduced by permission of Routledge, Inc., part of The Taylor & Francis Group.