The watersoluble gum fraction of myrrh (40% w/w), has been found to co
mprise of a heterodisperse mixture of proteoglycans with dominating am
ounts of uronic acid rich polymers. The major fraction (70% w/w) was a
proteoglycan (M(r) similar to 200 000) with protein content of 10% an
d Hyp as the main amino acid (40%). Structural investigations using mi
ld acid hydrolysis, Smith degradation and alkaline hydrolysis demonstr
ated that two different types of sugar chains are linked to the protei
n-core. These comprise either of short chains of arabinose or of sligh
tly branched chains composed of galactose and 4-O-methyl-glucuronic ac
id. Both structures are linked to the protein moiety via Hyp. As the g
alactose is substituted at C4 with 4-O-methyl-glucuronic acid, which i
s substituted at C2 with galactose, for this specific structure the te
rm ''4-O-methyl-glucurono-galactan'' is proposed. It has not yet been
reported in any other gum described so far. Gum myrrh containes furthe
rmore arabino-3.6-galactan-protein fractions with an average molecular
weight of about 70 000 and a protein amount of 31 and 16%, respective
ly. It can not be concluded whether the different types of proteoglyca
ns represent the naturally occurring diversity of polymers or whether
they derive from degradation processes during isolation or storage of
the commercial sample of myrrh, as it is used in the purview of the Eu
ropean Pharmacopea.