A Comprehensive Review of the Covalent Immobilization of Biomolecules onto Electrospun Nanofibers.

Biomolecule immobilization has attracted the attention of various fields such as fine chemistry and biomedicine for their use in several applications such as wastewater, immunosensors, biofuels, et cetera. The performance of immobilized biomolecules depends on the substrate and the immobilization method utilized. Electrospun nanofibers act as an excellent substrate for immobilization due to their large surface area to volume ratio and interconnectivity.

Biotin-Conjugated Cellulose Nanofibers Prepared via Copper-Catalyzed Alkyne-Azide Cycloaddition (CuAAC) "Click" Chemistry.

As potential high surface area for selective capture in diagnostic or filtration devices, biotin-cellulose nanofiber membranes were fabricated to demonstrate the potential for specific and bio-orthogonal attachment of biomolecules onto nanofiber surfaces. Cellulose acetate was electrospun and substituted with alkyne groups in either a one- or two-step process. The alkyne reaction, confirmed by FTIR and Raman spectroscopy, was dependent on solvent ratio, time, and temperature.

Translational regulation of proinsulin biosynthesis and proinsulin conversion in the pancreatic beta-cell.

Insulin secretion from the pancreatic beta -cell can be initiated in minutes, vary as much as 50-100-fold, and be sustained for several hours without need for changes in insulin gene transcription. Remarkably, the cellular content of the hormone and its molecular composition do not vary appreciably in the face of changes of insulin granule exocytosis. Minimal morphological changes are apparent, further indicating that the movement of lipids and membrane proteins between the granule storage pool, the plasma membrane, and Golgi are likewise tightly controlled.

Gene organization and alternative splicing of human prohormone convertase PC8.

The mammalian Ca2+-dependent serine protease prohormone convertase PC8 is expressed ubiquitously, being transcribed as 3.5, 4.3 and 6.

Genetically variable triplet repeats in a RING-finger ORF of Helicoverpa species baculoviruses.

Nucleotide sequence analysis of the Helicoverpa zea S-type nucleopolyhedrovirus (HzSNPV) genomic interval between the polh and iel genes has revealed an open reading frame (HOAR ORF) that contains a complex A 1-T rich triplet repeat region (RAT-repeats). HOAR ORF is predicted to encode an acidic, arginine residue rich. 712 aa protein, with a C3HC4 (RING-finger) zinc binding motif.

PC8 [corrected], a new member of the convertase family.

A novel subtilisin-like protein, PC8, was identified by PCR using degenerate primers to conserved amino acid residues in the catalytic region of members of the prohormone convertase family. PC8 was predicted to be 785 residues long and was structurally related to the mammalian convertases furin, PACE4, PC1 and PC2, sharing more than 50% amino acid identity over the catalytic region with these family members. PC8 possessed the catalytically important Asp, His, Asn and Ser amino acids, the homo B domain of this family of enzymes and a C-terminal hydrophobic sequence indicative of a transmembrane domain.

Nucleotide sequence of the polyhedrin gene region of Helicoverpa zea single nucleocapsid nuclear polyhedrosis virus: placement of the virus in lepidopteran nuclear polyhedrosis virus group II.

The polyhedrin gene (polh) of Helicoverpa zea single nucleocapsid nuclear polyhedrosis virus (HzSNPV) was identified and shown by sequence analysis of the EcoRI I genomic fragment to encode a 246 amino acid polypeptide that has greater than 80% sequence identity to known polyhedrins. It is preceded by an AT-rich region containing the conserved late promoter motif TAAG, which was identified as a transcription start point. Downstream of polh there were several similarities in genome arrangement to other nuclear polyhedrosis viruses (NPVs).