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Biomedical subjects

B Obrink

Publications and source records attributed to B Obrink.

83 records · Page 5Linked to original sources
PubMed1971

Nature of the interaction of chondroitin 4-sulphate and chondroitin sulphate-proteoglycan with collagen.

The electrostatic interaction of chondroitin sulphate and the chondroitin sulphate-proteoglycan with collagen was studied by chromatography of the glycosaminoglycan and the proteoglycan on a collagen gel. The observed binding between the macromolecules increased with decreasing pH and ionic strength, and was significant under physiological conditions. A study of the interaction between chondroitin sulphate and a preparation of soluble collagen, with a partition-equilibrium technique, afforded similar results.

Animals↗
PubMedDate not supplied

Expression of E-cadherin during craniofacial development.

The cell adhesion molecule E-cadherin is assumed to play an important role in organogenesis and histogenesis. We have analyzed the presence of E-cadherin during normal and disturbed craniofacial development with respect to palate and tooth formation by immunohistochemistry using a rat monoclonal antibody (DECMA-1) and by in situ hybridization using an oligonucleotide probe. Cleft palate was induced by retinoic acid (RA) treatment of pregnant dams. Normal and RA-treated fetuses of gestational days 14-18 were examined. E-cadherin was present in epithelia of both ectodermal and endodermal origin, including developing teeth and epithelia of the palate as well as respiratory and oral epithelia. The expression level of E-cadherin increased with age and differentiation. In normal fetuses, at day 18, the expression was higher in the epithelia of the oral cavity than in the forming nasal cavity. The expression pattern of E-cadherin implies that this molecule has a role during normal development of the epithelia of the craniofacial complex.

Animals↗
PubMedDate not supplied

Simultaneously synthesized peptides on continuous cellulose membranes as substrates for protein kinases.

Sets of peptides with defined sequences, each on a separate spot, were synthesized simultaneously on continuous cellulose membranes (SPOTs membranes), which were originally designed for epitope studies. The applicability of the membrane-bound peptides as substrates for protein kinases was tested using protein kinase A, protein kinase C and casein kinases I and II as model enzymes. We found that the peptide-membrane complexes can serve as kinase substrates. Our results suggest that membrane-bound peptides offer a new potential for the investigation of substrate specificity of protein kinases. An advantage to this method is that there is no need for substrate identification and separation, which is required with high-volume random peptide libraries. Membrane-bound peptides may even form a basis for kinase assays with peptides lacking multiple basic amino acids, required for separation of the substrates in conventional assays. Problems connected with protein kinase substrate specificity can be investigated in any laboratory using the rapid and inexpensive SPOTs technique, as neither costly apparatus nor special experience in peptide synthesis is necessary.

Amino Acid Sequence↗