Aug 1, 1995

Immunoblotting studies on artifactual contamination of enamel homogenates by albumin and other proteins

Calcified Tissue International
W ChenC E Smith


The reason for the presence of albumin and other serum, cytoskeletal, cytosolic, and extracellular matrix proteins in enamel fractions was investigated by immunoblotting using homogenates prepared from freeze-dried and freshly dissected rat incisors, and antibodies capable of resolving at least 1 ng of the primary antigen. The data indicated that most of the 16 antibodies examined in this study reacted with antigens present only within "cell" homogenates (enamel organ cells + adhering labial connective tissue and blood vessels). One exception was rat serum albumin which was detected routinely in enamel homogenates prepared from freshly dissected, wiped incisors but rarely within enamel homogenates prepared from freeze-dried incisors. Another exception was calbindin-D 28 kDa which was consistently found within secretory stage enamel homogenates irrespective of preparative technique. A third exception was enamel proteins (amelogenins) which were enriched in secretory and early maturation stage enamel homogenates compared with cell homogenates and distributed as multiple molecular weight, antigenic bands in enamel homogenates (14-30 kDa), but mostly as a single antigenic band in cell homogenates (near 27 kDa). Overall, the results...Continue Reading

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Mentioned in this Paper

Serum Albumin Measurement
Dental Enamel Proteins
Blood Vessel
Enamel Organ
Serum Proteins
Biologic Development
Morphologic Artifacts
Western Blot

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