Immunochemical Characterization of Porphyridium cruentum B-Phycoerythrin: Proof of Cross-Reaction between Chromophore-Free Apoprotein and Holoprotein-Specific Antibodies

نویسندگان

  • Eva Sepp
  • Gerhard Wanner
  • Jörg Eder
  • Hans-Peter Köst
چکیده

Antibodies against phycobilisom es o f Porphyridium cruentum immunoreact with B-phycoerythrin from the same organism. A strong antigen-antibody com plex is not only formed with the native B-phycoerythrin but also when the chromophore is chemically reduced, split or even degraded with chromic acid. Characteristics o f precipitations and dissolutions in the presence of the chaotropic reagents urea and potassium rhodanide are discussed for the immunocomplex with native B-phycoerythrin. A sandwich-type immunoadsorbent column appropriate for antigen-isolation is described; its binding properties are investigated biochem ically and by electron microscopy.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Recovery of pure B-phycoerythrin from the microalga Porphyridium cruentum.

Phycoerythrin is a major light-harvesting pigment of red algae and cyanobacteria that is widely used as a fluorescent probe and analytical reagent. In this paper, B-phycoerythrin and R-phycocyanin in native state, from the red alga Porphyridium cruentum were obtained by an inexpensive and simple process. The best results of this purification procedure were scaled up by a factor of 13 to a large...

متن کامل

Chromatographic purification and characterization of B-phycoerythrin from Porphyridium cruentum Semipreparative high-performance liquid chromatographic separation

A fast preparative two-step chromatographic method for purification of B-phycoerythrin from Porphyridium cruentum is described. This biliprotein was homogeneous as determined by sodium dodecyl sulfate–polyacrylamide gel electrophoresis yielding three closely migrating bands corresponding to its three subunits. Baseline separation of its a-, band g-subunits was achieved by a reversed-phase HPLC ...

متن کامل

Phycobilisome Structure of Porphyridium cruentum: POLYPEPTIDE COMPOSITION.

Purified phycobilisomes of Porphyridium cruentum were solubilized in sodium dodecyl sulfate and resolved by sodium dodecyl sulfate-acrylamide gel electrophoresis into nine colored and nine colorless polypeptides. The colored polypeptides accounted for about 84% of the total stainable protein, and the colorless polypeptides accounted for the remaining 16%. Five of the colored polypeptides rangin...

متن کامل

Effect of Pressure on the Absorption Spectra of Phycobiliprotein and Porphyridium cruentum

Changes in the absorption spectra o f P. cruentum and phycobiliprotein are observed as a function o f hydrostatic pressure. With phycobiliprotein both in solution and in algae, increasing hydrostatic pressure results in bathochromic shifts o f the absorption maxima. In addition, there is a splitting o f the absorption band of phycoerythrin. When P. cruentum is subjected to 250 bars there are in...

متن کامل

Effective Absorption Cross-Sections in Porphyridium cruentum: Implications for Energy Transfer between Phycobilisomes and Photosystem II Reaction Centers.

Effective absorption cross-sections for O(2) production by Porphyridium cruentum were measured at 546 and 596 nanometers. Although all photosystem II reaction centers are energetically coupled to phycobilisomes, any single phycobilisome acts as antenna for several photosystem II reaction centers. The cross-section measured in state I was 50% larger than that measured in state II.

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013