Related Experiment Video
Updated: May 3, 2026

08:36
AirID-Based Proximity Labeling for Protein-Protein Interaction in Plants
Published on: September 16, 2022
2.0K
Sieve-tube proteins from Cucurbita maxima.
J Beyenbach1, C Weber, H Kleinig
1Institut für Biologie II, Lehrstugl für Zellbiologie, Universität Freiburg, Schänzlestraße 9-15, D-7800, Freiburg i.Br., Federal Republic of Germany.
Planta
|January 21, 2014
Summary
Two major phloem proteins from pumpkin (Cucurbita maxima) were isolated and characterized. These basic proteins, with distinct molecular weights, represent a significant portion of the total phloem protein content.
Area of Science:
- Plant biochemistry
- Proteomics
- Molecular biology
Background:
- Phloem exudate contains essential proteins for plant transport and defense.
- Understanding pumpkin phloem proteins can reveal insights into plant physiology and intercellular communication.
Purpose of the Study:
- To isolate and characterize the main proteins found in the phloem exudate of Cucurbita maxima.
- To determine the molecular weight, amino acid composition, and structural properties of these proteins.
Main Methods:
- Ammonium-sulfate precipitation
- DEAE-cellulose chromatography
- Gel filtration
- Analytical ultracentrifugation
- SDS polyacrylamide gel electrophoresis
Main Results:
- Two major basic proteins (pI > 9.5) were isolated, each comprising ~40% of total protein.
- The smaller protein (MW ~30,000) readily dimerizes, likely its natural form.
- The larger protein (MW ~116,000) forms a gel without SH-protecting agents.
Conclusions:
- Cucurbita maxima phloem contains two predominant, highly basic proteins with distinct molecular weights.
- These proteins exhibit unique structural characteristics, including dimerization and gel formation.
- Further research into these proteins may elucidate their specific roles in phloem function.
Related Concept Videos
Protein Transport to the Inner Chloroplast Membrane
1.7K
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...
1.7K
Microtubule Associated Motor Proteins
10.0K
Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
10.0K
Overview of Secretory Vesicles
8.8K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.8K

