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Related Concept Videos

Photosystem I01:27

Photosystem I

Although structurally similar to photosystem II (PSII), photosystem I (PSI) is has a different electron supplier and electron acceptor.
Both these photosystems work in concert. An excited electron from PSII is relayed to PSI via an electron transport chain in the thylakoid membrane of the chloroplast, which is comprised of the carrier molecule plastoquinone, the dual-protein cytochrome complex, and plastocyanin. As electrons move between PSII and PSI, they lose energy and must be re-energized...
Photosystem II01:22

Photosystem II

The multi-protein complex photosystem II (PS II) harvests photons and transfers their energy through its bound pigments to its reaction center, and ultimately to photosystem I (PSI) through the electron transport chain. The pigments responsible for caputirng the light energy in photosystems include chlorophyll a, chlorophyll b, and carotenoids.
The pigment molecules are arranged across  two photosystem domains — the antenna complex and the reaction center. The main aim of the pigment molecules...
Photosystems01:32

Photosystems

Photosystems are multiprotein complexes that form the functional units of photosynthesis in plants, algae, and cyanobacteria. They are found embedded in the membrane of tiny sac-like structures called thylakoids placed inside the chloroplast.
Functioning of Photosystems
Photosystems contain many pigment molecules, such as chlorophylls and carotenoids, arranged in a particular organization across two domains — the antenna complex and the reaction center. The main aim of the pigment molecules...
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...

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Related Experiment Video

Updated: Jun 4, 2026

Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting
08:40

Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting

Published on: February 14, 2019

A novel membrane based process to isolate photosystem-I membrane complex from spinach.

Jianguo Liu1, Mengmeng Yin, Meng Wang

  • 1Center for Bioengineering and Biotechnology, China University of Petroleum (East China), Qingdao 266555, People's Republic of China. jianguoliu@upc.edu.cn

Photosynthesis Research
|January 29, 2011
PubMed
Summary

Researchers isolated photosystem-I (PS-I) using ultrafiltration, achieving high purity and activity recovery. This novel method offers an efficient way to isolate membrane proteins.

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Last Updated: Jun 4, 2026

Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting
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Area of Science:

  • Biochemistry
  • Membrane Protein Isolation
  • Biophysical Chemistry

Background:

  • Photosystem-I (PS-I) is crucial for photosynthesis.
  • Efficient isolation of membrane proteins like PS-I is challenging.
  • Ultrafiltration is a potential technique for protein purification.

Purpose of the Study:

  • To isolate photosystem-I (PS-I) from spinach using ultrafiltration.
  • To optimize ultrafiltration conditions for maximal PS-I purity and activity.
  • To evaluate ultrafiltration as a standalone method for membrane protein isolation.

Main Methods:

  • Ultrafiltration with 300 kDa polyethersulfone membranes.
  • Parameter scanning to optimize pH, ionic strength, stirring speed, and permeate flux.
  • O(2) electrode measurements to assess PS-I activity in the presence of detergents (Triton X-100, n-dodecyl-beta-D-maltoside).

Main Results:

  • Optimized ultrafiltration conditions yielded approximately 84% PS-I purity.
  • Activity recovery exceeded 94% post-ultrafiltration.
  • Demonstrated the effectiveness of ultrafiltration as a sole method for isolating a membrane protein.

Conclusions:

  • Ultrafiltration is a highly effective and efficient method for isolating photosystem-I (PS-I).
  • Optimized conditions ensure high purity and activity recovery of the isolated membrane protein.
  • This study presents the first report of membrane protein isolation solely through ultrafiltration.