{"title":"对蛇毒及其毒素的质谱研究","authors":"K. Tubbs, R. Nelson, J. R. Krone, A. Bieber","doi":"10.1081/TXR-100100313","DOIUrl":null,"url":null,"abstract":"The profound effect of Biological Mass Spectrometry (MS) on protein analysis has been amplified by recent developments in analytically based matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF MS). This review provides a brief synapses of snake toxin based research allocating mass spectrometric immunoassay (MSIA) and bioreactive probe tips technologies. Contingent upon advances in Biological MS has been the movement of mass spectrometric applications into array based technology. Biomolecular interaction analysis interfaced with mass spectrometry (BIA/MS) exemplifies the diverse potential of chip based techniques, combining the powerful front-end analysis of biological interaction events with the dynamic precision of MALDI-MS mass specific assignment, to demonstrate “lab on a chip” technology. Analysis of other snake venoms and related toxins by electrospray ionization and tandem mass spectrometry as well as capillary electrophoresis combined with MALDI-MS are included. The development of new and powerful mass spectral methods for the study of biopolymers have increased substantially in recent years. Matrix-assisted laser desorption ionization (MALDI) , secondary ion , electrospray , and tandem mass spectrometry are among the mass spectral techniques that have been used to study biopolymers . Mass spectrometry, when combined with the mass spectrometric immunoassay, enzymatically active probe elements and biomolecular interaction analysis, has given rise to a number powerful bio-analytical methods for protein studies. Fig. explores some of the ways in which these approaches are being applied in protein analysis. The methods, which are rapid, sensitive and accurate, can be used to study pure proteins, complex mixtures of proteins and selected proteins in a complex mixture. The study of toxins and proteins from snake venoms by mass spectrometric techniques has been rather limited, even though the new techniques appear ideally suited for examining complex mixtures of proteins commonly found in snake venoms. This review of the current literature will summarize work in which mass spectrometric techniques have been successfully applied to the study of venoms and proteins obtained from them. The review will not be totally inclusive, but will illustrate some of the ways that mass spectrometric techniques have been used in researching venoms and proteins. The focus of the review will be on studies of myotoxins and neurotoxins acquired from rattlesnake venoms, thus illustrating the systematic use of several mass spectrometry based techniques for analyzing intrinsic venom proteins. Figure 1. Overview of biological mass spectrometry applied to the study of snake toxin proteins.","PeriodicalId":17561,"journal":{"name":"Journal of Toxicology-toxin Reviews","volume":"6 1","pages":"1 - 22"},"PeriodicalIF":0.0000,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"5","resultStr":"{\"title\":\"MASS SPECTRAL STUDIES OF SNAKE VENOMS AND SOME OF THEIR TOXINS\",\"authors\":\"K. Tubbs, R. Nelson, J. R. Krone, A. Bieber\",\"doi\":\"10.1081/TXR-100100313\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The profound effect of Biological Mass Spectrometry (MS) on protein analysis has been amplified by recent developments in analytically based matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF MS). This review provides a brief synapses of snake toxin based research allocating mass spectrometric immunoassay (MSIA) and bioreactive probe tips technologies. Contingent upon advances in Biological MS has been the movement of mass spectrometric applications into array based technology. Biomolecular interaction analysis interfaced with mass spectrometry (BIA/MS) exemplifies the diverse potential of chip based techniques, combining the powerful front-end analysis of biological interaction events with the dynamic precision of MALDI-MS mass specific assignment, to demonstrate “lab on a chip” technology. Analysis of other snake venoms and related toxins by electrospray ionization and tandem mass spectrometry as well as capillary electrophoresis combined with MALDI-MS are included. The development of new and powerful mass spectral methods for the study of biopolymers have increased substantially in recent years. Matrix-assisted laser desorption ionization (MALDI) , secondary ion , electrospray , and tandem mass spectrometry are among the mass spectral techniques that have been used to study biopolymers . Mass spectrometry, when combined with the mass spectrometric immunoassay, enzymatically active probe elements and biomolecular interaction analysis, has given rise to a number powerful bio-analytical methods for protein studies. Fig. explores some of the ways in which these approaches are being applied in protein analysis. The methods, which are rapid, sensitive and accurate, can be used to study pure proteins, complex mixtures of proteins and selected proteins in a complex mixture. The study of toxins and proteins from snake venoms by mass spectrometric techniques has been rather limited, even though the new techniques appear ideally suited for examining complex mixtures of proteins commonly found in snake venoms. This review of the current literature will summarize work in which mass spectrometric techniques have been successfully applied to the study of venoms and proteins obtained from them. The review will not be totally inclusive, but will illustrate some of the ways that mass spectrometric techniques have been used in researching venoms and proteins. The focus of the review will be on studies of myotoxins and neurotoxins acquired from rattlesnake venoms, thus illustrating the systematic use of several mass spectrometry based techniques for analyzing intrinsic venom proteins. Figure 1. Overview of biological mass spectrometry applied to the study of snake toxin proteins.\",\"PeriodicalId\":17561,\"journal\":{\"name\":\"Journal of Toxicology-toxin Reviews\",\"volume\":\"6 1\",\"pages\":\"1 - 22\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2000-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Toxicology-toxin Reviews\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1081/TXR-100100313\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Toxicology-toxin Reviews","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1081/TXR-100100313","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
MASS SPECTRAL STUDIES OF SNAKE VENOMS AND SOME OF THEIR TOXINS
The profound effect of Biological Mass Spectrometry (MS) on protein analysis has been amplified by recent developments in analytically based matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF MS). This review provides a brief synapses of snake toxin based research allocating mass spectrometric immunoassay (MSIA) and bioreactive probe tips technologies. Contingent upon advances in Biological MS has been the movement of mass spectrometric applications into array based technology. Biomolecular interaction analysis interfaced with mass spectrometry (BIA/MS) exemplifies the diverse potential of chip based techniques, combining the powerful front-end analysis of biological interaction events with the dynamic precision of MALDI-MS mass specific assignment, to demonstrate “lab on a chip” technology. Analysis of other snake venoms and related toxins by electrospray ionization and tandem mass spectrometry as well as capillary electrophoresis combined with MALDI-MS are included. The development of new and powerful mass spectral methods for the study of biopolymers have increased substantially in recent years. Matrix-assisted laser desorption ionization (MALDI) , secondary ion , electrospray , and tandem mass spectrometry are among the mass spectral techniques that have been used to study biopolymers . Mass spectrometry, when combined with the mass spectrometric immunoassay, enzymatically active probe elements and biomolecular interaction analysis, has given rise to a number powerful bio-analytical methods for protein studies. Fig. explores some of the ways in which these approaches are being applied in protein analysis. The methods, which are rapid, sensitive and accurate, can be used to study pure proteins, complex mixtures of proteins and selected proteins in a complex mixture. The study of toxins and proteins from snake venoms by mass spectrometric techniques has been rather limited, even though the new techniques appear ideally suited for examining complex mixtures of proteins commonly found in snake venoms. This review of the current literature will summarize work in which mass spectrometric techniques have been successfully applied to the study of venoms and proteins obtained from them. The review will not be totally inclusive, but will illustrate some of the ways that mass spectrometric techniques have been used in researching venoms and proteins. The focus of the review will be on studies of myotoxins and neurotoxins acquired from rattlesnake venoms, thus illustrating the systematic use of several mass spectrometry based techniques for analyzing intrinsic venom proteins. Figure 1. Overview of biological mass spectrometry applied to the study of snake toxin proteins.