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(3) ¦L¨ê¥»¡y»Ã¯À¤Æ¾Ç¹êÅç¡z¤¤¨Ã¨S¦³¦¬¿ý ®Ö»Ä³¡¥÷¡A¦]¦¹¤]¨S¦³½s¤J¥»¯Á¤Þ¡C |
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Manometry ´úÀ£ªk, 142 Map, laboratory layout ¹êÅç«Ç°t¸m¹Ï, 234-235 Mass spectrum ½èÃлö¤ÀªR, 69, 157, 166-167 Maximum velocity, see Vmax Mechanism, catalysis ¶Ê¤Æ¾÷¨î, 84-85 Medline [°Ó«~¦W] Âå¾Ç¸ê®Æ®w, 30, 35 Membrane protein ½¤³J¥Õ½è, 114 Meme Äj, 54 Mercaptoethanol, beta ²¸¾J°ò¤A¾J, 114, 129, 139, 144, 152, 199, 208 Mercuric chloride (HgCl2) ´â¤Æ¨E, 216 MES (2[N-morpholino] ethanesulfonic acid) ¶ÜªL¤A°òÁD»Ä, 215 Metabolic regulation ¥NÁ½ձ±, 92 Metal ª÷ÄÝ, 74, 82, 84-85, 88, 123, 130, 143-146 Metal chelating affinity chromatography (MCAC) [°Ó«~¦W] ª÷ÄÝîg¦X¼hªRªk, 130 Metal protease ª÷ÄݳJ¥Õ×Q, 75, 84, 88 Metallothionein (MT) ª÷Äݲ¸¨O, 158 Methanesulfonic acid ¥ÒÖJÁD»Ä, 158 Methanogen ¥ÒÖJµß, 52 Methanol ¥Ò¾J, 212-214, 216, 217-221 Methionine (Met, M) ¥Ò²¸Ói»Ä, 58-59, 85, 161 Michaelis and Menten, 76 Michaelis-Menten constant, see Km Michaelis-Menten equation, °Ê¤O¾Ç¤½¦¡, 77-80, 91 Microanalysis ·L¶q¤ÀªR, 166 Microbodies ·LÊ^, 53 Microsome ·L²ÉÊ^, 53 Microtiter plate ·L¶qºw©w½L, 28, 193-198 Mitochondria ²É½uÊ^, 53, 94 Mobile phase ¬y°Ê¬Û, 118-119, 124, 128, 131 Molar extinction coefficient ¤À¤l®ø¥ú«Y¼Æ, 140, 161 Molecular activity, see Turnover number Molecular cloning ¤À¤l¿ï´Þ, 65, 95 Molecular weight determination ¤À¤l¶q´ú©wªk, 69, 156-157 Molecular weight standards ¼Ð·Ç¤À¤l¶q²Õ¦X, disc-PAGE ìºA¹qªa¼Ð·Ç²Õ, 206 gel filtration ½¦Åé¹LÂo¼Ð·Ç²Õ, 6-7, 156 gradient PAGE ±è«×¹qªa¼Ð·Ç²Õ, 157 SDS-PAGE, SDS ¹qªa¼Ð·Ç²Õ, 8-13, 208, 217 Western transfer ¹qªaÂà¦L¼Ð·Ç²Õ, 12-13, 217 Monoclonal antibody ³æ®è§ÜÅé, 162-163, 227 Myoglobin ¦Ù¬õ³J¥Õ, 66-67, 211, 217 Myosin ¦Ù¾®³J¥Õ, 217 |
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NAD+, NADH (nicotinamide adenine dinucleotide) µÒÆPñQÓi¸¢áIËï¤G®Ö¥Ì»Ä, 75, 130, 141-142 Native PAGE, see Disc-PAGE NBT (nitro blue tetrazolium) ´áÂÅ¥|¾V, 219-220 Negative cooperativity ¥¿¨ó¦P§@¥Î, 67 Nickel Âì, 130 Nitrilotriacetic acid îg¦X¾¯, 130 Nitrocellulose µv¤ÆÅÖºû¯È, 154 NMR (nuclear magnetic resonance) ®ÖºÏ¦@®¶, 69, 161 N-OH-succinimide ¬¡¤Æ«¬¿Ë©M¤ÏÀ³°ò¹Î, 129 Non-competitive inhibition «DÄvª§©Ê§í¨î, 83 NS-1, myeloma cell °©ÅèÀù²ÓM, 163 N-terminal determination, N-ºÝ©w§Ç, 158-160, 167, 220-221 Nuclear region ®Ö°Ï, 52 Nucleic acid ®Ö»Ä, (¦L¨ê¥»¡y»Ã¯À¤Æ¾Ç¹êÅç¡z¤¤¨S¦³¦¬¿ý®Ö»Ä³¡¥÷) Nylon ¥§Às½¤, 154 |
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Octyl Sepharose [°Ó«~¦W] HIC ½¦Åé, 130 One-Page Show ¤@¶³ø§i, 2-3, 33, 38, 41-41, 232, 243, 245 Operon ¾ÞÁa¤l, 93 Organelle M¾¹, 52-53, 94, 113 Organic solvent precipitation ¦³¾÷·»¾¯¨I¾ýªk, 116-117 Origin of Life ¥Í©R·½°_, 51, 75 Ovalbumin §Z¥Õ³J¥Õ, 156 Oxirane ¿Ë©M§lµÛ¾¯¤ÏÀ³°ò¹Î, 129 |
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PABA (p-amino benzoic acid) ¹ïÓi°òf¥Ò»Ä, 82 Particle size, gel ¤¶½è²É¤l¤j¤p, 120-121, 132 Partition ¼hªR²G¬Û¤À°t, 118-119, 130-131 Partitioning ²G¬Û¤À°t, 131 PAS staining, PAS ÁÞ¬V¦â, 153, 214-215 PBS (phosphate buffered saline) ÁC»Ä¥Í²z¹ÆQ¤ô, 218-220 PBST (phosphate buffered saline and Tween) ¥[ Tween ÁC»Ä¥Í²z¹ÆQ¤ô, 219-220 PC/GENE [°Ó«~¦W] §Ç¦C¤ÀªR³nÅé, 30, 159, 162, 167, 224, 226 PCMB (p-cholro-mercuricbenzoate), ¹ï´âf¥Ò»Ä (Cys³J¥Õ×Q§í¨î¾¯), 82 PEG (polyethylene glycol) »E¤A²m¤A¤G¾J, 116 Penicillin «CÅð¯À, 82 Peptide Ð`¨O, 59, 61, 65, 67, 70, 74, 84, 87-88, 148, 158-161, 162, 167 Peptide bond Ð`Áä, 59, 65, 158-159 Peptide mapping Ð`¨O¹ÏÃÐ, 148, 160 Peptidoglycan Ð`¨O»EÁÞ, 52 P-E-R-D system ¹êÅç°O¿ý¨t²Î, 32, 36-38, 242 Periodic acid ¹L¸K»Ä, 214 Periodic acid-Schiff's reagent, see PAS staining Peroxisome ¹L®ñ¤Æ×QÅé, 53 PEST site, PEST °¸Ñ«H¸¹, 159, 224-227, 251 pH »ÄÆP«×, buffer ½w½Ä²G, 54, 60-61, 111, 144-146 electrophoresis ¹qªa, 150-151, 153 enzyme activity ¹ï¬¡©Ê¼vÅT, 68-69, 95, 112-115, 146 ion exchange Â÷¤l¥æ´«ªk, 125-128 protein extraction ³J¥Õ½è©â¨ú, 112-115 pH meter »ÄÆP«×p, 25, 110, 142, 144 Phenol oxidase ×ô®ñ¤Æ×Q, 114 Phenolic compound §t×ô¤Æ¦Xª«, 114 Phenyl Sepharose [°Ó«~¦W] HIC ¤¶½è, 130 Phenylalanine (Phe, F) f¤þÓi»Ä, 58-59, 85, 161 Phosphatase ÁC»Ä×Q, 89, 143-144, 218-220 Phosphate buffer ÁC»Ä½w½Ä²G, 144-145 Phosphate, inorganic (Pi) µL¾÷ÁC»Ä, 143, 195-198 Phosphomolybdic-phosphotungstate ÁCà»»Ä-ÁCÂë»Ä, 139-140 Phosphoric acid ÁC»Ä, 211 Phosphorylase b ¨x¿}ÁC¸Ñ×Q b, 208, 224-228 Phosphorylation ÁC»Ä¤Æ, 89, 224-227 pI (isoelectric point) µ¥¹qÂI, 60-61, 64, electrophoresis ¹qªa, 147, 157, 205 ion exchange Â÷¤l¥æ´«, 125-126, 128 isoelectric focusing µ¥¹qµJ¶°ªk, 69, 128, 155, 210-211 Pili ÅÖ¤ò, 52 PITC (phenylisothiocyanate) f²§²¸Ùæ»ÄÆQ, 70, 159 Plastid M½èÊ^, 53 PMSF (phenylmethylsulfonyl fluoride) f¥Ò°òÁDñQ¤Æ¬t, 145-146 Polyacrylamide »E¤þ²mñQÓi, 149, 205 Polybuffer [°Ó«~¦W] IEF ½w½Ä²G, 127-128 Polyproline II helix »E²ãÓi»ÄÁ³±Û II, 66, 224-226, 251 Polytron [°Ó«~¦W] °ª®Ä¯à§¡½è¾÷, 113 Ponceau ¬V¦â¾¯, 155 Positive cooperativity ¥¿¨ó¦P§@¥Î, 67 Potassium chloride (KCl) ´â¤Æ¹[, 153-154 Potassium iodide (KI) ¸K¤Æ¹[, 215 Power supply ¹q·½¨ÑÀ³¾¹, 205 PPC (paper partition chromatography) Âo¯È¤À°t¦âªRªk, 118, 142 Precursor «eÅXÅé, 87 Preparative electrophoresis »s³Æ¦¡¹qªa, 2, 10-11, 133, 148, 203-204 Primary structure ¤@¯Åºc³y, 64-65, 159 Pristane °´ÓÖJ, 163 Prokaryote ì®Ö²ÓM, 51-52 Proline (Pro, P) ²ãÓi»Ä, 58-59, 64, 66, 224-226 Proplastid «eM½èÅé, 53 Prosthetic group »²°ò, 67, 160 Protamine sulfate ³½ºë³J¥Õ, 117, 138 Proteases ³J¥Õ½è¤ô¸Ñ×Q, 70, 82-83, 88, 146, 160-161 Proteasome ³J¥Õ×QÅé, 88-89, 93 Protein ³J¥Õ½è, 65, structure analysis ³J¥Õ½èºc³y¤ÀªR, 69-70, 158-161, 166-167 Protein A ³J¥Õ½è A, 130 Protein assay ³J¥Õ½è©w¶qªk, 69, 139-140, 193-194 Protein engineering ³J¥Õ½è¤uµ{, 96 Protein extraction ³J¥Õ½è©â¨ú, 112-117 Protein kinase ³J¥Õ½è¿E×Q, 89 Protein technology ³J¥Õ½è¬ì§Þ, 69, 165-168 Protein transfer, see Western transfer Proteolytic cleavage ³J¥Õ½èµõ¸Ñ, 87-89, 161 Proteome ³J¥Õ½èÅé, 96, 167-168 Prothrombin ¾®¦å×Qì, 87 Pulse field gel electrophoresis ¯ß½Ä³õ½¦Åé¹qªa, 148 Pump, peristaltic į°ÊÀ°®ú, 201 Purification fold ¯Â¤Æ¿²v, 137-138 Purification strategy ¯Â¤Æµ¦²¤, 137-138 Purification table ¯Â¤Æªí, 14-15, 138 Purification techniques ³J¥Õ½è¯Â¤Æ§Þ³N, 69, 105-138 PVDF (polyvinylidene difluoride) Âà¦L¯È, 217-221 |
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Ramachandran plot ¤G¯Åºc³y¹w´ú¹Ï, 66 Random coil ¥ô·N§Î, 66 Reagent ¸Õ¾¯, 110 Reference Manager [°Ó«~¦W] ¤åÄm¸ê®Æ®w³nÅé, 30, 35 Regulation ¬¡©Ê½Õ¸`, 87-91 Relaxed form ÃP´²«¬, 91 Report format ³ø§i®æ¦¡, 39-40 Report writing ³ø§i¼¶¼g, 40-41 Reporter ³ø¾ÉªÌ, 95 Reservoir ¶J¦s¼Ñ, 121-122 Reverse osmosis °fº¯³z, 135 Reverse phase chromatography ¤Ï¬Û¼hªRªk, 118, 130-131, 138, 161 Riboflavin (vitamin B2) ®Ö¶À¯À, 149 Ribonuclease, see RNase Ribosome ®Ö¿}Ê^, 52 RNase (ribonuclease) ®Ö¿}®Ö»Äúê, 67, 142 Rotor Â÷¤ßÂàªû, 26-27, 134-135 Rule, laboratory ¹êÅç«Ç³W«h, 33 |
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