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J. Biol. Chem., Vol. 263, Issue 21, 10240-10246, 07, 1988
A Oohira, F Matsui, M Matsuda, Y Takida and Y Kuboki
More than 60% of brain chondroitin sulfate proteoglycans were extracted
from 10-day-old rat brains by homogenization in ice-cold phosphate-
buffered saline containing protease inhibitors. Although the soluble
proteoglycan preparation was a mixture of chondroitin sulfate proteoglycans
with a different hydrodynamic size as well as a different molecular
density, each subfraction of the proteoglycans contained chondroitin
sulfate side chains with virtually identical molecular weight
(approximately 15,000) and chondroitin sulfate disaccharide composition
(high content of 4-sulfate unit). Digestion of the purified proteoglycan
preparation with protease-free chondroitinase ABC produced five core
proteins with Mr = 250,000 (designated as 250K protein), 220,000 (220K),
150,000 (150K), 130,000 (130K), and 93,000 (93K). All these core proteins
were obtained from chondroitin sulfate proteoglycan preparations extracted
from various regions of the brain, but their composition varied among
different brain regions. Analysis for amino acid composition of these core
proteins and two-dimensional mapping of their proteolytic peptides revealed
that three major core proteins (250K, 220K, and 150K proteins) were
structurally different. These observations indicate that at least three
distinct types of chondroitin sulfate proteoglycan occur in the developing
rat brain.
Occurrence of three distinct molecular species of chondroitin sulfate proteoglycan in the developing rat brain
Department of Embryology, Institute for Developmental Research, Aichi, Japan.
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