rimorphin and 4-hydroxymercuribenzoate

rimorphin has been researched along with 4-hydroxymercuribenzoate* in 2 studies

Other Studies

2 other study(ies) available for rimorphin and 4-hydroxymercuribenzoate

Article	Year
Differential effects of N-peptidyl-O-acyl hydroxylamines on dynorphin-induced antinociception in the mouse capsaicin test. Neuropeptides, 2005, Volume: 39, Issue:6 In the capsaicin test, intrathecal (i.t.) dynorphins are antinociceptive. Cysteine protease inhibitors such as p-hydroxymercuribenzoate (PHMB) given i.t. augment and prolong their activity. The effect of two novel cysteine protease inhibitors, N-peptidyl-O-acyl hydroxylamines, on the antinociception induced by i.t. administered dynorphin A or dynorphin B has been investigated. When administered i.t. 5 min before the injection of capsaicin (800 ng) into the plantar surface of the hindpaw, dynorphin A (62.5-1000 pmol) or dynorphin B (0.5-4 nmol) produced a dose-dependent and significant antinociceptive effect. The effect of dynorphin A (1 nmol) and dynorphin B (4 nmol) disappeared completely within 180 and 60 min, respectively. PHMB (2 nmol) and Boc-Tyr-Gly-NHO-Bz (BYG-Bz) (2 nmol) co-administered with dynorphin A or dynorphin B significantly prolonged antinociception induced by both. On the other hand, Z-Phe-Phe-NHO-Bz (ZFF-Bz) (1 and 2 nmol) only prolonged antinociception induced by dynorphin A. The results suggest that Z-Phe-Phe-NHO-Bz is an inhibitor of cysteine proteases preferring cleavage of dynorphin A, with less specificity towards dynorphin B in the mouse spinal cord. Topics: Analgesics; Animals; Capsaicin; Dynorphins; Endorphins; Humans; Hydroxylamines; Hydroxymercuribenzoates; Injections, Spinal; Male; Mice; Pain Measurement; Protease Inhibitors	2005
Isoforms of a dynorphin B converting enzyme isolated by column electrophoresis in agarose suspension. Biochemistry international, 1991, Volume: 23, Issue:1 A dynorphin B converting enzyme previously purified from bovine spinal cord was subjected to column electrophoresis in agarose suspension. By this technique combined with HPLC gel filtration it was possible to resolve and recover several isoforms of the proteinase. All these isoenzymes were associated with a similar molecular size but apparently they differed with regard to their net charges. No significant difference between their inhibitory profiles or their Km values for the release of Leu-enkephalin-Arg6 from dynorphin B was observed. Topics: Animals; Cattle; Chromatography, Gel; Chromatography, High Pressure Liquid; Cysteine Endopeptidases; Dynorphins; Electrophoresis, Agar Gel; Endorphins; Enkephalin, Leucine; Hydroxymercuribenzoates; Isoelectric Point; Isoenzymes; Kinetics; Molecular Weight; Spinal Cord	1991

Article

Year

Differential effects of N-peptidyl-O-acyl hydroxylamines on dynorphin-induced antinociception in the mouse capsaicin test.

Neuropeptides, 2005, Volume: 39, Issue:6

In the capsaicin test, intrathecal (i.t.) dynorphins are antinociceptive. Cysteine protease inhibitors such as p-hydroxymercuribenzoate (PHMB) given i.t. augment and prolong their activity. The effect of two novel cysteine protease inhibitors, N-peptidyl-O-acyl hydroxylamines, on the antinociception induced by i.t. administered dynorphin A or dynorphin B has been investigated. When administered i.t. 5 min before the injection of capsaicin (800 ng) into the plantar surface of the hindpaw, dynorphin A (62.5-1000 pmol) or dynorphin B (0.5-4 nmol) produced a dose-dependent and significant antinociceptive effect. The effect of dynorphin A (1 nmol) and dynorphin B (4 nmol) disappeared completely within 180 and 60 min, respectively. PHMB (2 nmol) and Boc-Tyr-Gly-NHO-Bz (BYG-Bz) (2 nmol) co-administered with dynorphin A or dynorphin B significantly prolonged antinociception induced by both. On the other hand, Z-Phe-Phe-NHO-Bz (ZFF-Bz) (1 and 2 nmol) only prolonged antinociception induced by dynorphin A. The results suggest that Z-Phe-Phe-NHO-Bz is an inhibitor of cysteine proteases preferring cleavage of dynorphin A, with less specificity towards dynorphin B in the mouse spinal cord.

Topics: Analgesics; Animals; Capsaicin; Dynorphins; Endorphins; Humans; Hydroxylamines; Hydroxymercuribenzoates; Injections, Spinal; Male; Mice; Pain Measurement; Protease Inhibitors

2005

Isoforms of a dynorphin B converting enzyme isolated by column electrophoresis in agarose suspension.

Biochemistry international, 1991, Volume: 23, Issue:1

A dynorphin B converting enzyme previously purified from bovine spinal cord was subjected to column electrophoresis in agarose suspension. By this technique combined with HPLC gel filtration it was possible to resolve and recover several isoforms of the proteinase. All these isoenzymes were associated with a similar molecular size but apparently they differed with regard to their net charges. No significant difference between their inhibitory profiles or their Km values for the release of Leu-enkephalin-Arg6 from dynorphin B was observed.

Topics: Animals; Cattle; Chromatography, Gel; Chromatography, High Pressure Liquid; Cysteine Endopeptidases; Dynorphins; Electrophoresis, Agar Gel; Endorphins; Enkephalin, Leucine; Hydroxymercuribenzoates; Isoelectric Point; Isoenzymes; Kinetics; Molecular Weight; Spinal Cord

1991