Peptide Libraries in T‐Cell‐Mediated Immune Response

Fleckenstein, Burkhard; Jung, Günther; Wiesmüller, Karl‐Heinz

doi:10.1002/9783527613502.ch11

Cited by 2 publications

(1 citation statement)

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“…1997) revealed no sequence identities with relevant proteins. Synthetic peptides were prepared by multiple solid‐phase peptide synthesis on a robotic system (Syro MultiSynTech, Bochum, Germany) using fluorenylmethoxycarbonyl/t‐butyl (Fmoc/tBu) chemistry and 2‐chlorotrityl resin (Senn Chemicals, Dielsdorf, Switzerland) (Jung and Beck‐Sickinger 1992; Fleckenstein et al . 1999).…”

Section: Selection and Synthesis Of Isozyme‐specific Oligopeptidesmentioning

confidence: 99%

Immunocytochemical localization of glycogen phosphorylase isozymes in rat nervous tissues by using isozyme‐specific antibodies

Pfeiffer-Guglielmi¹,

Fleckenstein

Jung

et al. 2003

Journal of Neurochemistry

151

172

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Isozyme-specific antibodies were raised against peptides from the low-homology regions of the sequences of rat glycogen phosphorylase BB and MM isozymes by immunization of rabbits and guinea pigs. Immunocytochemical double-labelling experiments on frozen sections of rat nervous tissues were performed to investigate the isozyme localization pattern. Astrocytes throughout the brain and spinal cord expressed both isozymes in perfect co-localization. Ependymal cells only expressed the BB isozyme. Most neurones were not immunoreactive. The rare neurones that contained glycogen phosphorylase only expressed the BB isozyme. Nearly all of these neurones formed part of the afferent somatosensory system. These findings stress the general importance of glycogen in neural energy metabolism and indicate a special role for the glycogen phosphorylase BB isozyme in neurones in the somatosensory system.

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Section: Selection and Synthesis Of Isozyme‐specific Oligopeptidesmentioning

confidence: 99%