Oriented immobilization of PNgase F on a porous polymer monolith for rapid N-glycan release

We demonstrate a simple and rapid method for the oriented immobilization of peptide-N4-(Nacetyl- glucosaminyl) asparagine amidase F (PNGase F) on a porous polymer monolith. The oriented immobilization is based on the affinity of glutathione-S-transferase (GST) tagged PNGase F towards glutathione modified monolith prepared in the capillary format. This approach allows the oriented and easily replaceable immobilization of PNGase F for rapid and efficient release of N-linked glycans. The reactor was tested by deglycosylation of several native glycoproteins such as ribonuclease B, fetuin or human immunoglobulin G. The proteins were effectively deglycosylated in several minutes and the released N-linked glycans were analyzed using off-line MALDI/MS or CE/LIF

Development of an opening-tearing mode fracture system for composite materials

In this paper the mixed-mode I/III prestressed split-cantilever beam fracture specimen [1,2] is developed, which combines the mode-III modified split-cantilever beam [1] and the well-known double-cantilever beam [3] specimens using a special rig. The most important feature of the novel beam-like specimen is that it is able to provide any combinations of the mode-I and mode-III energy release rates. If only crack propagation onset is involved then the mixed-mode I/III prestressed split-cantilever beam specimen can be used to obtain the fracture criterion of transparent composite materials in the GI – GIII plane in a relatively simple way