1) Taking myosin light chain kinase (MLCK) activity as the index, bovine extract was fractionated by the use of anion-exchange chromatography, cation-exchange chromatography, and calmodulin affinity chromatography. The kinase activity of the fraction thus obtained was elevated up to about 12,400 times over that of the original crude extract. 2) The fraction mentioned above was subjected again to anion exchange chromatography. The kinase activities were divided into two parts, i.e., part I which contained the 155 kDa component and part II which was virtually free of 155 kDa component. The MLCK activity of part I was considerably lower than that of part II. 3) Part I was subjected to gel filtration using AcA 34 gel and the 155 kDa component was isolated. The fraction contained the 155 kDa component in a homogeneous state and showed myosin specific kinase activity, which was about 2 X 10(5) times that of the original crude extract. 4) The high kinase activity of part II seemed to be ascribable to the 130 kDa component, in accord with the report of Hathaway, Adelstein, and Klee (J. Biol. Chem. 256, 8183-8189, 1981).
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122564 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Large and Stable Nanopores Formed by Complement Component 9 for Characterizing Single Folded Proteins.
ACS Nano
January 2025
Adolphe Merkle Institute, University of Fribourg, Fribourg 1700, Switzerland.
Biological nanopores offer a promising approach for single-molecule analysis of nucleic acids, peptides, and proteins. The work presented here introduces a biological nanopore formed by the self-assembly of complement component 9 (C9). This exceptionally large and cylindrical protein pore is composed of 20 ± 4 monomers of C9 resulting in a diameter of 10 ± 4 nm and an effective pore length of 13 nm.
View Article and Find Full Text PDFSERS profiling of blood serum filtrate components from patients with type II diabetes using 100 kDa filtration devices.
RSC Adv
January 2025
Département de Chimie, Faculté des Sciences et de Génie, Université Laval Québec QC G1V 0A6 Canada.
Blood carries some of the most valuable biomarkers for disease screening as it interacts with various tissues and organs in the body. Human blood serum is a reservoir of high molecular weight fraction (HMWF) and low molecular weight fraction (LMWF) proteins. The LMWF proteins are considered disease marker proteins and are often suppressed by HMWF proteins during analysis.
View Article and Find Full Text PDFResonant Young's Slit Interferometer for Sensitive Detection of Low-Molecular-Weight Biomarkers.
Biosensors (Basel)
January 2025
School of Physics, Engineering and Technology, University of York, York YO10 5DD, UK.
The detection of low-molecular-weight biomarkers is essential for diagnosing and managing various diseases, including neurodegenerative conditions such as Alzheimer's disease. A biomarker's low molecular weight is a challenge for label-free optical modalities, as the phase change they detect is directly proportional to the mass bound on the sensor's surface. To address this challenge, we used a resonant Young's slit interferometer geometry and implemented several innovations, such as phase noise matching and optimisation of the fringe spacing, to maximise the signal-to-noise ratio.
View Article and Find Full Text PDFStructural analysis of sulfated fucan from the sea cucumber Holothuria mexicana with the assistance of endo-1,3-fucanase.
Carbohydr Polym
March 2025
State Key Laboratory of Marine Food Processing & Safety Control, College of Food Science and Engineering, Ocean University of China, 1299 Sansha Road, Qingdao 266404, China.
Sulfated fucan from sea cucumber has received growing interest in recent decades. Insight into the primary structure of sulfated fucan is fundamental to elucidate their bioactivity. The sea cucumber Holothuria mexicana possesses a high market demand, while the structure of its sulfated fucan (Hm-FUC) remains unclear.
View Article and Find Full Text PDFEvaluation of TOCSY mixing for sensitivity-enhancement in solid-state NMR and application of 4D experiments for side-chain assignments of the full-length 30 kDa membrane protein GlpG.
J Biomol NMR
January 2025
Research Unit Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Robert- Rössle-Straße 10, 13125, Berlin, Germany.
Chemical shift assignments of large membrane proteins by solid-state NMR experiments are challenging. Recent advancements in sensitivity-enhanced pulse sequences, have made it feasible to acquire H-detected 4D spectra of these challenging protein samples within reasonable timeframes. However, obtaining unambiguous assignments remains difficult without access to side-chain chemical shifts.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!