Læknablaðið - 15.04.1983, Page 4

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NÝR DOKTOR í LÆKNISFRÆÐI - STEFÁN KARLSSON
Nýlega varöi Stefán Karlsson doktorsritgerð
sína við Lundúnaháskóla. Hér fer á eftir
útdráttur úr ritgerðinni, en heiti hennar er
Biochemical and genetical aspects of glyco-
proteins in human tissues.
Abstract
Glycoproteins from human tissues and body
fluids have been examined by SDS polyacryla-
mide gel electrophoresis and isoelectric focus-
ing followed by staining with various radioio-
dinated lectins with different carbohydrate
binding specificities. The main aim of the study
was to make use of these techniques for
biochemical and genetic analysis of glycopro-
teins in health and disease.
Considerable differences were found in the
glycoprotein profiles detected by many lectins,
from one tissue to another. Differences were
also observed between membrane-rich and
soluble fractions of each tissue. Serum pro-
teins were detected in both fractions of post
mortem tissues and were a considerable pro-
portion of the glycoproteins seen in the
soluble fractions.
With peanut agglutinin a glycoconjugate
was detected in urine, lung and kidney which
shows genetically determined polymorphism.
Family studies and population genetic data
indicate that it is inherited in an autosomal co-
dominant manner. Four common alleles have
been detected so far. This glycoconjugate has
been compared with Tamm-Horsfall (TH)
glycoprotein, and found to have different
lectin binding and electrophoretic mobility but
it has a similar lictin binding and electrophore-
tic mobility to a urinary mucin described and
characterized recently by Cartron. It is sugge-
sted that the urinary mucin and the polymor-
phic glycoconjugate are the same and the
molecule is referred to as the peanut aggluti-
nin reactive urinary mucin (PUM).
Preparations of TH glycoprotein purified
from various individuals who are positive with
respect to the Sd blood group (Sd(a + )) react
with soy bean agglutinin whereas Sd(a —)
individuals do not. Electrophoretic differences
were seen in TH glycoproteins from different
individuals but the evidence suggests that
these variations reflect modifications of non-
genetic nature.
Glycoproteins from cystic fibrosis (CF) pa-
tients have been compared with those of
healthy controls and heterozygous individuals.
Serum, red cell membranes, cultured fibro-
blasts and urine have been analysed with SDS
electrophoresis and urine and serum have also
been investigated using isoelectric focusing.
The gels have been stained with ten lectins but
no CF specific glycan changes have been
detected.