Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Golgi Apparatus01:49

Golgi Apparatus

108.1K
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
108.1K
Golgi Apparatus01:09

Golgi Apparatus

22.8K
Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
22.8K
Golgi Apparatus01:09

Golgi Apparatus

4.9K
4.9K
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

2.6K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.6K
Transport Across the Golgi01:26

Transport Across the Golgi

6.7K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
6.7K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

3.4K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
3.4K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Genome-wide identification and functional characterization of the CaD27 gene family in pepper under cold stress.

Plant molecular biology·2026
Same author

Golgi Fragmentation as a Potential Link Between SARS-CoV-2 Infection and Alzheimer's Disease: Mechanisms and Implications for Neurodegeneration in Long COVID.

Sub-cellular biochemistry·2026
Same author

Beyond the Secretory Pathway: New Insights Into Protein Release.

Traffic (Copenhagen, Denmark)·2025
Same author

SARS-CoV-2 remodels the Golgi apparatus to facilitate viral assembly and secretion.

PLoS pathogens·2025
Same author

GRASP55 regulates sorting and maturation of the lysosomal enzyme β-hexosaminidase A.

Molecular biology of the cell·2025
Same author

Identification of the CaCRT gene family and function of CaCRT1 under low-temperature stress in pepper (Capsicum annuum L.).

Scientific reports·2025
Same journal

High-Throughput Microbial Assay for Amino Acid Measurement in Ground Maize Seed Samples Utilizing Auxotrophic <i>E. coli</i>.

Cold Spring Harbor protocols·2025
Same journal

Grain Quality in Maize.

Cold Spring Harbor protocols·2025
Same journal

High-Throughput Assay for Measuring Phytate and Available Phosphorus in Ground Maize Seed Samples.

Cold Spring Harbor protocols·2025
Same journal

Functional Genomic Analysis of Transposon Insertion Mutant Maize Plants from the UniformMu National Public Resource.

Cold Spring Harbor protocols·2025
Same journal

The UniformMu National Public Resource: Transposon<i>-</i>Induced Mutant Seeds for Functional Genomics Studies in Maize.

Cold Spring Harbor protocols·2025
Same journal

Insights from the Study of B<i>-</i>Cell Epitopes of a Microbial Pathogen by Phage Display.

Cold Spring Harbor protocols·2025
See all related articles

Related Experiment Video

Updated: Apr 11, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

11.5K

Golgi isolation.

Danming Tang1, Yanzhuang Wang1

  • 1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109.

Cold Spring Harbor Protocols
|June 3, 2015
PubMed
Summary
This summary is machine-generated.

This study details a method for isolating Golgi apparatus membranes from rat liver cells. The protocol uses sucrose gradients to purify Golgi stacks, crucial for understanding cellular protein and lipid transport.

More Related Videos

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation
14:44

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation

Published on: March 14, 2014

13.5K
Isolation of Primary Mouse Retinal Glial M&#252;ller Cells
04:39

Isolation of Primary Mouse Retinal Glial Müller Cells

Published on: August 30, 2024

3.3K

Related Experiment Videos

Last Updated: Apr 11, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

11.5K
Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation
14:44

Isolation of mRNAs Associated with Yeast Mitochondria to Study Mechanisms of Localized Translation

Published on: March 14, 2014

13.5K
Isolation of Primary Mouse Retinal Glial M&#252;ller Cells
04:39

Isolation of Primary Mouse Retinal Glial Müller Cells

Published on: August 30, 2024

3.3K

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • The Golgi apparatus is a vital organelle for modifying and packaging proteins and lipids.
  • Studying Golgi structure and function requires isolating these membranes from cellular homogenates.
  • Liver cells are ideal sources due to their high Golgi membrane content from active secretion.

Purpose of the Study:

  • To establish a reliable protocol for purifying Golgi apparatus membranes.
  • To assess the yield and structural integrity of isolated Golgi stacks.

Main Methods:

  • Rat liver homogenate was subjected to two sequential sucrose gradient centrifugations.
  • Golgi membrane purification was achieved using differential centrifugation techniques.
  • Enzyme activity of β-1,4-galactosyltransferase, a Golgi marker, was measured to assess purity.

Main Results:

  • The protocol yielded Golgi membranes purified 80- to 100-fold compared to the initial homogenate.
  • A significant majority (60%-70%) of the isolated Golgi structures retained their characteristic stacked morphology.
  • Increased activity of the marker enzyme confirmed successful enrichment of Golgi membranes.

Conclusions:

  • This sucrose gradient method provides an efficient means to isolate purified Golgi apparatus membranes.
  • The protocol preserves the structural integrity of Golgi stacks, making them suitable for further functional studies.
  • The findings facilitate research into Golgi apparatus roles in cellular transport and secretion.