+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Refined purification and characterization of Z-protein

Refined purification and characterization of Z-protein

Journal of Biochemistry 106(1): 110-114

Using an improved procedure, Z-protein was prepared from myofibrils of chicken breast muscle. The yield of pure Z-protein increased to 10 mg per kg of muscle. The chain weight of Z-protein was 55,000 in the presence of SDS. However, Z-protein was eluted before aldolase (Mr 158,000) in Sephacryl S-400 column chromatography, and, therefore, it appeared to exist as a tetramer in a physiological salt solution. Z-protein had at least four isopeptides whose isoelectric points ranged from pH 6.0 to 6.4. Anti-Z-protein antiserum reacted equally with these isopeptides. The extinction coefficient of Z-protein at wavelength 278 nm was 4.2 (1%; light path, 1 cm). Z-protein which was purified according to this improved method did not bind to F-actin and alpha-actinin in a physiological salt solution.

Please choose payment method:

(PDF emailed within 1 workday: $29.90)

Accession: 041202220

Download citation: RISBibTeXText

PMID: 2777742

Related references

Refined Purification and Characterization of Z-Protein1. The Journal of Biochemistry 106(1): 110-114, 1989

Affinity purification and refined structural characterization of terminal deoxynucleotidyltransferase. Biochemical Journal 231(1): 105-113, 1985

Refined purification of large amounts of rat cvHsp/HspB7 and partial biological characterization in vitro. Protein and Peptide Letters 21(5): 503-510, 2014

Refined purification and further characterization of oxygen evolving and tris treated photosystem ii particles from the thermophilic cyanobacterium synechococcus sp. Biochimica et Biophysica Acta 936(3): 307-318, 1988

The accuracy of refined protein structures comparison of 2 independently refined models of bovine trypsin. Acta Crystallographica Section B Structural Crystallography & Crystal Chemistry 35(8): 1861-1874, 1979

Acuracy of refined protein structures. II. Comparison of four independently refined models of human interleukin 1beta. Acta Crystallographica. Section D, Biological Crystallography 50(Pt 6): 808-812, 1994

Quantification and partial characterization of the residual protein in fully and partially refined commercial soybean oils. Journal of Agricultural and Food Chemistry 59(5): 1752-1759, 2011

Refined characterization of head and neck squamous cell carcinomas expressing a seemingly wild-type p53 protein. Journal of Oral Pathology and Medicine 35(1): 19-24, 2006

A real-time and hands-on research course in protein purification and characterization: Purification and crystal growth of human inosine triphosphate pyrophosphatase. Biochemistry and Molecular Biology Education 39(1): 28-37, 2011

Structural proteins of rinderpest virus ii purification and characterization of the nucleocapsid protein n the hemagglutinin protein h and the matrix protein m. Indian Journal of Biochemistry & Biophysics 25(6): 574-579, 1988

Purification and characterization of Mr 43,000 protein similar to Mr 25,000 protein, a substrate for protein Ser/Thr kinases, identified as a part of Xenopus laevis vitellogenin B1. Journal of Protein Chemistry 22(6): 571-583, 2003

Purification and characterization of a Ca2+/calmodulin-dependent protein kinase II from hog gastric mucosa using a protein-protein affinity chromatographic technique. European Journal of Biochemistry 255(2): 516-525, 1998

Regulation of Protein Synthesis in Plant Embryo by Protein Phosphorylation : I. Purification and Characterization of a cAMP-Independent Protein Kinase and Its Endogenous Substrate. Plant Physiology 83(4): 988-993, 1987

Regulation of protein synthesis in plant embryo by protein phosphorylation i. purification and characterization of a cyclic amp independent protein kinase and its endogenous substrate. Plant Physiology 83(4): 988-993, 1987

The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. Journal of Molecular Biology 269(1): 142-153, 1997