Purification, phosphate content and phosphorylation of myosin from human vascular smooth muscle.

S. Fazekas, G. Nádasy, E. Monos, A. G. Kovách, V. Székessy-Hermann

Research output: Contribution to journalArticle

Abstract

Myosin was prepared from human umbilical artery and some of its properties were studied. The yield of myosin after ultracentrifugation was 4.3-13.6 mg/gr wet weight of tissue (mean: 8.6 mg/gr). A considerable amount of phosphate bound to the myosin was found in all preparations. Phosphate content of umbilical arterial myosin was higher than what had been found in our earlier works in skeletal muscle myosin. Phosphate content of umbilical arterial myosin also could be further increased by incubation in ATP containing media. While the rate of phosphorylation of human umbilical arterial myosin was slower than that of skeletal muscle myosin, the saturated phosphate levels reached with 0.5 mM ATP concentration were higher for vascular myosin. The slower phosphate uptake rate of vascular myosin may be related to the slower contraction rate of this muscle type. After alkaline hydrolysis of lipid free myosin, 7 or 8 peaks of N-phosphoryl amino acids and phosphorylated amino acid derivates could be separated by ion exchange chromatography.

Original languageEnglish
Pages (from-to)23-33
Number of pages11
JournalActa Physiologica Hungarica
Volume72
Issue number1
Publication statusPublished - 1988

Fingerprint

Myosins
Vascular Smooth Muscle
Phosphates
Phosphorylation
Umbilicus
Skeletal Muscle Myosins
Blood Vessels
Adenosine Triphosphate
Amino Acids
Umbilical Arteries
Ultracentrifugation
Ion Exchange Chromatography
Muscle Contraction
Hydrolysis
Lipids
Weights and Measures

ASJC Scopus subject areas

  • Physiology

Cite this

Purification, phosphate content and phosphorylation of myosin from human vascular smooth muscle. / Fazekas, S.; Nádasy, G.; Monos, E.; Kovách, A. G.; Székessy-Hermann, V.

In: Acta Physiologica Hungarica, Vol. 72, No. 1, 1988, p. 23-33.

Research output: Contribution to journalArticle

@article{0af27b15aefb4689b1cc3dcb4f29038c,
title = "Purification, phosphate content and phosphorylation of myosin from human vascular smooth muscle.",
abstract = "Myosin was prepared from human umbilical artery and some of its properties were studied. The yield of myosin after ultracentrifugation was 4.3-13.6 mg/gr wet weight of tissue (mean: 8.6 mg/gr). A considerable amount of phosphate bound to the myosin was found in all preparations. Phosphate content of umbilical arterial myosin was higher than what had been found in our earlier works in skeletal muscle myosin. Phosphate content of umbilical arterial myosin also could be further increased by incubation in ATP containing media. While the rate of phosphorylation of human umbilical arterial myosin was slower than that of skeletal muscle myosin, the saturated phosphate levels reached with 0.5 mM ATP concentration were higher for vascular myosin. The slower phosphate uptake rate of vascular myosin may be related to the slower contraction rate of this muscle type. After alkaline hydrolysis of lipid free myosin, 7 or 8 peaks of N-phosphoryl amino acids and phosphorylated amino acid derivates could be separated by ion exchange chromatography.",
author = "S. Fazekas and G. N{\'a}dasy and E. Monos and Kov{\'a}ch, {A. G.} and V. Sz{\'e}kessy-Hermann",
year = "1988",
language = "English",
volume = "72",
pages = "23--33",
journal = "Physiology International",
issn = "2498-602X",
publisher = "Akademiai Kiado",
number = "1",

}

TY - JOUR

T1 - Purification, phosphate content and phosphorylation of myosin from human vascular smooth muscle.

AU - Fazekas, S.

AU - Nádasy, G.

AU - Monos, E.

AU - Kovách, A. G.

AU - Székessy-Hermann, V.

PY - 1988

Y1 - 1988

N2 - Myosin was prepared from human umbilical artery and some of its properties were studied. The yield of myosin after ultracentrifugation was 4.3-13.6 mg/gr wet weight of tissue (mean: 8.6 mg/gr). A considerable amount of phosphate bound to the myosin was found in all preparations. Phosphate content of umbilical arterial myosin was higher than what had been found in our earlier works in skeletal muscle myosin. Phosphate content of umbilical arterial myosin also could be further increased by incubation in ATP containing media. While the rate of phosphorylation of human umbilical arterial myosin was slower than that of skeletal muscle myosin, the saturated phosphate levels reached with 0.5 mM ATP concentration were higher for vascular myosin. The slower phosphate uptake rate of vascular myosin may be related to the slower contraction rate of this muscle type. After alkaline hydrolysis of lipid free myosin, 7 or 8 peaks of N-phosphoryl amino acids and phosphorylated amino acid derivates could be separated by ion exchange chromatography.

AB - Myosin was prepared from human umbilical artery and some of its properties were studied. The yield of myosin after ultracentrifugation was 4.3-13.6 mg/gr wet weight of tissue (mean: 8.6 mg/gr). A considerable amount of phosphate bound to the myosin was found in all preparations. Phosphate content of umbilical arterial myosin was higher than what had been found in our earlier works in skeletal muscle myosin. Phosphate content of umbilical arterial myosin also could be further increased by incubation in ATP containing media. While the rate of phosphorylation of human umbilical arterial myosin was slower than that of skeletal muscle myosin, the saturated phosphate levels reached with 0.5 mM ATP concentration were higher for vascular myosin. The slower phosphate uptake rate of vascular myosin may be related to the slower contraction rate of this muscle type. After alkaline hydrolysis of lipid free myosin, 7 or 8 peaks of N-phosphoryl amino acids and phosphorylated amino acid derivates could be separated by ion exchange chromatography.

UR - http://www.scopus.com/inward/record.url?scp=0023798011&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023798011&partnerID=8YFLogxK

M3 - Article

C2 - 3421126

AN - SCOPUS:0023798011

VL - 72

SP - 23

EP - 33

JO - Physiology International

JF - Physiology International

SN - 2498-602X

IS - 1

ER -