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crystallization of human erythrocyte anion channel protein and circular dichroism spectroscopy of bacillus thuringiensis-insecticide and magainin-like antibiotics (endotoxins, toxins). [microform]
crystallization of human erythrocyte anion channel protein and circular dichroism spectros...
crystallization of human erythrocyte anion channel protein and circular dichroism spectroscopy of bacillus thuringiensis-insecticide and magainin-like antibiotics (endotoxins, toxins). [microform]

상세정보

자료유형  
 마이크로피시
청구기호  
540 V471c
    저자명  
    서명/저자  
    crystallization of human erythrocyte anion channel protein and circular dichroism spectroscopy of bacillus thuringiensis-insecticide and magainin-like antibiotics (endotoxins, toxins). - [microform]
    발행사항  
    형태사항  
    336 p. : microfiches ; 11×15 cm.
    총서명  
    UMI Dissertation
    주기사항  
    Source: Dissertation Abstracts International, Volume: 53-07, Section: B, page: 3462.
    학위논문주기  
    thesis (ph.d.)-- - rensselaer polytechnic institute, 1992.
    초록/해제  
    요약The main goal of this thesis work is the structural studies of three types of biopolymers in order to elucidate the correlation between structure and function. Several physical and chemical methods were used to study the $\delta$-endotoxin from insecticide Bacillus thuringiensis (BT), the antibiotics magainin and PGLa, and human erythrocyte anion channel protein, also known as Band 3.
    초록/해제  
    요약Delta-Endotoxin is a paracrystalline protein (protoxin) produced by BT. Toxins from different subspecies of BT kill different classes of insects. Subspecies Kurstaki used for the present studies, kills insect larvae belonging to the class Lepidopteran upon ingestion. The protoxin is cleaved to produce a toxin molecule in the gut of the insect. Circular dichroism (CD) spectroscopy and gel-electrophoresis (SDS-PAGE) were used to study the conformation of both the protoxin and the toxin molecules. It was found that both these proteins undergo conformational changes with varying pH and these changes may be correlated with pH-dependent change in the toxic activity of BT.
    초록/해제  
    요약PGLa and magainin are 21-residue and 23-residue polypeptide antibiotics. CD spectroscopy was used to examine the conformation of these molecules in a variety of environments, as a basis for understanding their structural features. In addition, phospholipid binding studies were used to demonstrate features which permit the association of these polypeptides with membranes. These studies suggest that channels formed from a bundle of helices may be appropriate models for both of these antibiotics.
    초록/해제  
    요약Band 3 is the 95 kDa integral membrane glycoprotein of the erythrocyte membrane. This protein is responsible for the exchange of chloride and bicarbonate across the erythrocyte cell membranes. Band 3 was isolated and purified from red blood cell membranes. Various techniques such as high pressure liquid size exclusion chromatography, SDS-PAGE and CD spectroscopy were used to characterize the purified protein. The protein was crystallized out of detergent solution. A number of morphologically distinct microcrystals (dimensions $\sim$0.3 x 0.05 x 0.2 mm) were prepared (Venugopal & Wallace, 1990). Preliminary diffraction studies indicate that while they are disordered, they do diffract to 3 A resolution.
    복제주기  
    Microfiche : UMI . microfiches;11×15 cm.
    일반주제명  
    일반주제명  
    일반주제명  
    키워드  
    기타저자  
    기본자료저록  
    Dissertation Abstracts International. 53-07B.

    MARC

     008970923s1992        us                                    eng
    ■001MOKWON00232997
    ■001AAV9236249
    ■00520010328155859
    ■008970923s1992        us                                    eng    
    ■035    ▼a(UnM)AAV9236249
    ■040    ▼aUnM▼cUnM▼dMOKWON
    ■090    ▼a540▼bV471c
    ■1001  ▼avenugopal,  manju  grover.
    ■24510▼acrystallization  of  human  erythrocyte  anion  channel  protein  and  circular  dichroism  spectroscopy  of  bacillus  thuringiensis-insecticide  and  magainin-like  antibiotics  (endotoxins,  toxins).▼h[microform]
    ■260    ▼aU.S.▼brensselaer  polytechnic  institute▼c1992.
    ■300    ▼a336  p.▼bmicrofiches▼c11×15  cm.
    ■350    ▼a$50.6
    ■44000▼aUMI  Dissertation
    ■500    ▼aSource:  Dissertation  Abstracts  International,  Volume:  53-07,  Section:  B,  page:  3462.
    ■502    ▼athesis  (ph.d.)--▼brensselaer  polytechnic  institute▼d1992.
    ■520    ▼aThe  main  goal  of  this  thesis  work  is  the  structural  studies  of  three  types  of  biopolymers  in  order  to  elucidate  the  correlation  between  structure  and  function.    Several  physical  and  chemical  methods  were  used  to  study  the  $\delta$-endotoxin  from  insecticide  Bacillus  thuringiensis  (BT),  the  antibiotics  magainin  and  PGLa,  and  human  erythrocyte  anion  channel  protein,  also  known  as  Band  3.
    ■520    ▼aDelta-Endotoxin  is  a  paracrystalline  protein  (protoxin)  produced  by  BT.    Toxins  from  different  subspecies  of  BT  kill  different  classes  of  insects.    Subspecies  Kurstaki  used  for  the  present  studies,  kills  insect  larvae  belonging  to  the  class  Lepidopteran  upon  ingestion.    The  protoxin  is  cleaved  to  produce  a  toxin  molecule  in  the  gut  of  the  insect.    Circular  dichroism  (CD)  spectroscopy  and  gel-electrophoresis  (SDS-PAGE)  were  used  to  study  the  conformation  of  both  the  protoxin  and  the  toxin  molecules.    It  was  found  that  both  these  proteins  undergo  conformational  changes  with  varying  pH  and  these  changes  may  be  correlated  with  pH-dependent  change  in  the  toxic  activity  of  BT.
    ■520    ▼aPGLa  and  magainin  are  21-residue  and  23-residue  polypeptide  antibiotics.    CD  spectroscopy  was  used  to  examine  the  conformation  of  these  molecules  in  a  variety  of  environments,  as  a  basis  for  understanding  their  structural  features.    In  addition,  phospholipid  binding  studies  were  used  to  demonstrate  features  which  permit  the  association  of  these  polypeptides  with  membranes.    These  studies  suggest  that  channels  formed  from  a  bundle  of  helices  may  be  appropriate  models  for  both  of  these  antibiotics.
    ■520    ▼aBand  3  is  the  95  kDa  integral  membrane  glycoprotein  of  the  erythrocyte  membrane.    This  protein  is  responsible  for  the  exchange  of  chloride  and  bicarbonate  across  the  erythrocyte  cell  membranes.    Band  3  was  isolated  and  purified  from  red  blood  cell  membranes.    Various  techniques  such  as  high  pressure  liquid  size  exclusion  chromatography,  SDS-PAGE  and  CD  spectroscopy  were  used  to  characterize  the  purified  protein.    The  protein  was  crystallized  out  of  detergent  solution.    A  number  of  morphologically  distinct  microcrystals  (dimensions  $\sim$0.3  x  0.05  x  0.2  mm)  were  prepared  (Venugopal  &  Wallace,  1990).    Preliminary  diffraction  studies  indicate  that  while  they  are  disordered,  they  do  diffract  to  3  A  resolution.
    ■533    ▼aMicrofiche▼cUMI▼emicrofiches;11×15  cm.
    ■590    ▼aSchool  code:  0185.
    ■650  4▼aChemistry,  Biochemistry
    ■650  4▼aBiophysics,  General
    ■650  4▼aChemistry,  General
    ■653    ▼acrystallization▼aof▼ahuman▼aerythrocyte▼aanion▼achannel▼aprotein▼aand▼acircular▼adichroism▼aspectroscopy▼aof▼abacillus▼athuringiensis-insecticide▼aand▼amagainin-like▼aantibiotics▼a(endotoxins▼atoxins).
    ■690    ▼a0487
    ■690    ▼a0786
    ■690    ▼a0485
    ■71020▼arensselaer  polytechnic  institute.
    ■7730  ▼tDissertation  Abstracts  International▼g53-07B.
    ■790    ▼a0185
    ■791    ▼aPH.D.
    ■792    ▼a1992

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