摘要: Publisher Summary The chapter discusses three major groups of hydrolases, namely, proteases, nucleases and carbohydrases. Deoxyribonucleases can be inhibited by chelating agents if metal-dependent, moving the pH or ionic strength outside working range, low concentrations denaturants, gentle heating. Ribonucleases are renowned for their robustness very difficult to inhibit. Two commercially available inhibitors, vanadyl ribonucleosides rat placental ribonuclease inhibitor, generally effective but because they do not covalently modify protein, little use in denaturing systems. If reactive group at active site is known, then it may modification with a group-specific reagent, example, iodoacetamide thiol nucleases. Metal-dependent enzymes agents. A number chemical inhibitors ribonucleases many these bind nucleic acids prevent enzyme from acting simply steric effects against other acid metabolizing enzymes; used must carefully titrated.
sci-hub.se 参考文章(64)
P Scudder, K Uemura, J Dolby, M N Fukuda, T Feizi, Isolation and characterization of an endo-β-galactosidase from Bacteroides fragilis Biochemical Journal. ,vol. 213, pp. 485- 494 ,(1983) , 10.1042/BJ2130485
L. Ehrenberg, I. Fedorcsak, F. Solymosy, Diethyl pyrocarbonate in nucleic acid research. Progress in Nucleic Acid Research and Molecular Biology. ,vol. 16, pp. 189- 262 ,(1976) , 10.1016/S0079-6603(08)60758-8
Elliott Shaw, [58] Site-specific reagents for chymotrypsin, trypsin, and other serine proteases Methods in Enzymology. ,vol. 25, pp. 655- 660 ,(1972) , 10.1016/S0076-6879(72)25062-5
Christian Betzel, Gour P. Pal, Mark Struck, Klaus-Dieter Jany, Wolfram Saenger, Active-site geometry of proteinase K FEBS Letters. ,vol. 197, pp. 105- 110 ,(1986) , 10.1016/0014-5793(86)80307-6
Ewa Marciniak, Factor‐Xa Inactivation by Antithrombin III British Journal of Haematology. ,vol. 24, pp. 391- 400 ,(1973) , 10.1111/J.1365-2141.1973.TB01662.X
A Anastasi, M A Brown, A A Kembhavi, M J H Nicklin, C A Sayers, D C Sunter, A J Barrett, Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. Biochemical Journal. ,vol. 211, pp. 129- 138 ,(1983) , 10.1042/BJ2110129
SHOKICHI OHUCHI, HIROYUKI SUDA, HIROSHI NAGANAWA, KENJI KAWAMURA, TAKAAKI AOYAGI, HAMAO UMEZAWA, Structure-activity relationships among derivatives of arphamenines, inhibitors of aminopeptidase B. The Journal of Antibiotics. ,vol. 37, pp. 1741- 1743 ,(1984) , 10.7164/ANTIBIOTICS.37.1741
Klaus-Dieter JANY, Barbara MAYER, Proteinase K from Tritirachium album limber. I. Molecular mass and sequence around the active site serine residue. Biological chemistry Hoppe-Seyler. ,vol. 366, pp. 485- 492 ,(1985) , 10.1515/BCHM3.1985.366.1.485
Wojciech Ardelt, Michael Laskowski, Turkey ovomucoid third domain inhibits eight different serine proteinases of varied specificity on the same ...Leu18-Glu19... reactive site Biochemistry. ,vol. 24, pp. 5313- 5320 ,(1985) , 10.1021/BI00341A007
Tadazumi Komiyama, Hiroyuki Suda, Takaaki Aoyagi, Tomio Takeuchi, Hamao Umezawa, Kooichi Fujimoto, Sumio Umezawa, Studies on inhibitory effect of phosphoramidon and its analogs on thermolysin Archives of Biochemistry and Biophysics. ,vol. 171, pp. 727- 731 ,(1975) , 10.1016/0003-9861(75)90085-5