• Korean Journal of Food Science and Technology
• /
• v.7 no.4
• /
• pp.221-228
• /
• 1975

Meat tenderness is one of the most important factors in meat products because it plays a major role in the palatability of meat. To get information on the role of commercial meat tenderizer, the tenderizing ability of commercial meat tenderizer was measured with various substrates. The results obtained are as follows. 1. Content of crude protein in a commercial meat tenderizer was 4.9%. 2. Optimum temperature for proteolytic activity of meat tenderizer was $60{\sim}70^{\circ}C$. 3. Maximal activity of proteinase was obtained at pH $6{\sim}7$. 4. Proteolytic enzyme was activated by KCN, NaCN, EDTA. Thus, it was concluded that protease system of commercial meat tenderizer composed of plant origin proteinases. 5. Proteinase activity was completely inhibited by 10mM of N-Ethylmaleimide. 6. Commercial meat tenderizer showed stronger proteolytic activity on casein than on the water soluble fraction of meat protein, whereas it hydrolyzed the myofibrillar protein less efficiently.

• Parasites, Hosts and Diseases
• /
• v.33 no.3
• /
• pp.211-218
• /
• 1995

To clarify the correlation of the proteinase activity with pathogenicity of Clonorrhis sinensis, the proteinase activity either in excretory-secretory products (ESP) or in crude extracts of adult C. sinensis was examined. Substrate gel electrophoresis of the ESP and crude extracts revealed four distinct enzyme bands, which were differently inhibited by the specific proteinase inhibitors. The proteinase of the ESP with molecular mass of 24 kDa, was purified 23-fold with 14.5% yield by spectra gel ACA 44 gel filtration. It exhibited optimal pH at 7.5 in sodium phosphate (0.1 M). Its activity was inhibited specifically by N-ethylmaleimide (NEMI and antipain whereas potentiated 1.9 folds in the presence of 5 mM dithiothreitol (DTT). Cytotoxicity of the proteinase increased in a dose- dependent manner up to 120 ㎍/ml while reduced by NEM and antipain, indicating that cysteine proteinase was responsible for the cytotoxicity. This result shows that the 24 kDa cysteine proteinase is deeply correlated with the pathogenicity of C. sinensis infection.

• The Korean Journal of Pharmacology
• /
• v.32 no.1
• /
• pp.23-29
• /
• 1996

According to the traditional receptor model, competitive antagonists share with agonists the ability to bind to a common site on receptors, but they are different from agonist in that they cannot trigger the biological response-i.e., they lack intrinsic efficacy. Recent findings extend the model by indicating that not all antagonists display an intrinsic efficacy of zero but that some display 'inverse agonism'. In the present study we studied the inverse agonism at $A_1$ adenosine receptors in membranes prepared from rat cerebral cortex. Eight commercially available $A_1$ adenosine receptor antagonists (CGS-15943, ADPX, CPT, DPCPX, DPX, N-0840, PACPX and 8-PT) were screened for inverse agonism by measuring the extent of $[^{35}S]guanosine-5'-({\gamma}-thio)$ triphosphate $([^{35}S]GTP_{\gamma}S)$ binding to G proteins. The agonist-induced stimulation of $[^{35}S]GTP_{\gamma}S$ bindings was completely blocked in the presence of $A_1$ adenosine receptor antagonists. Under optimal conditions, two types of antagonists could be distinguished. Seven antagonists including DPCPX decreased the basal $[^{35}S]GTP_{\gamma}S$ binding in the absence of agonist, displaying inverse agonist activity. One (CGS-15943) had no effect on the basal bindings. N-ethylmaleimide treatment reduced the basal bindings as well as agonist-mediated stimulation of $[^{35}S]GTP_{\gamma}S$ bindings, indicating that a substantial amount of this binding reflects an activated state of the C proteins. In good agreement with these findings, 0.1 mM GTP decreased the apparent affinity of the receptors for the agonist PIA, increased that for DPCPX, and had no effect on that for CGS-15943.

• Korean Journal of Food Science and Technology
• /
• v.27 no.6
• /
• pp.909-914
• /
• 1995

In order to investigate gelation properties of Gelation Properties of ${\alpha}-lactalbumin$(${\alpha}-La$), gelling times and protein solubilities of ${\alpha}-La$ gels prepared in 0.1 M Tris-HCI buffer(pH 8.0) followed by heating at $90^{\circ}C$ for 40 minutes under different ${\alpha}-La$ concentration, NaCl, $CaCl_2$, N-ethylmaleimide(NEM), and dithiothreitol(DTT) concentration were measured. Gelling times decreased with increasing concentration of ${\alpha}-La$, NaCl, $CaCl_2$, and DTT, but increased with increasing concentration of NEM. ${\alpha}-La$ solutions made from all treatments were gelled within 40 minutes with the exception of NEM at $20{\sim}50\;mM$. Solubilities decreased with increasing concentration of ${\alpha}-La$, NaCl, $CaCl_2$, and DTT, but the solubility of NEM-modified gels increased with increasing concentration of NEM. As the results, solubilities In standard buffer were $10.4{\sim}51.3%$, $9.2{\sim}35.4%$, $11.1{\sim}35.0%$, $8.0{\sim}9.5%$, and $96.8{\sim}56.2%$, respectively. Solubilities in standard buffer containing 8 M urea and 0.5% SDS were higher than those in standard buffer, and were $41.8{\sim}81.3%$, $41.9{\sim}64.1%$, $43.5{\sim}69.8%$, $29.6{\sim}38.5%$, and $77.4{\sim}98.9%$, respectively. Solubilities in the presence of DTT were almost close to 100% in all conditions. These results indicates that the gelation rate and solubility are influenced by many factors, i.e. protein concentration, kind and concentration of salts, concentration of thiol reagents. The solubility of gel decreased with increasing the gelation rate.