scholarly journals Action of Dinitrophenyl Amino Acids on Skeletal Muscle Proteins II. Absorption of Bis-Dinitrophenyl-Lysine By Light and Heavy Meromyosins and by Light Meromyosin Fraction I

1968 ◽  
Vol 21 (1) ◽  
pp. 141
Author(s):  
RW Burley ◽  
WJH Jackson ◽  
Jean P Robertson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Ionic Strength ◽  
High Speed ◽  
Equilibrium Dialysis ◽  
The Other ◽  
Muscle Proteins ◽  
Heavy Meromyosin ◽  
Skeletal Muscle Proteins ◽  
Fraction I

The quantity of bis(2,4-dinitrophenyl)-L-Iysine (abbreviation bis-DNP-Iysine) absorbed at 5�C by myosin and meromyosins of rabbit skeletal muscle was estimated in phosphate buffer (pH 7, ionic strength 0�5) by two methods, one based on equilibrium dialysis, the other on high-speed centrifugation. According to both methods, heavy meromyosin absorbed more of the reagent than did the same weight of the parent myosin; light meromyosin absorbed less, and light meromyosin fraction I absorbed less still. There were, however, relatively large quantitative differences between the two methods, possibly because of an effect of the slightly different conditions of treatment.

scholarly journals Action of Dinitrophenyl Amino Acids on Skeletal Muscle Proteins

1969 ◽  
Vol 22 (1) ◽  
pp. 205
Author(s):  
RW Burley ◽  
Jean P Robertson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Equilibrium Dialysis ◽  
Total Absorption ◽  
Muscle Proteins ◽  
Heavy Meromyosin ◽  
Skeletal Muscle Myosin ◽  
Skeletal Muscle Proteins ◽  
Sulphydryl Groups ◽  
Muscle Myosin

Isotherms for the total absorption ofbis(2,4-dinitrophenyl)-L-lysine (bis-DNP-lysine) by rabbit skeletal muscle myosin and heavy meromyosin whose sulphydryl groups had been progressively blocked with p-chloromercuribenzoate were measured by equilibrium dialysis in Tris buffers containing potassium chloride.

scholarly journals Action of Dinitrophenyl Amino Acids on Skeletal Muscle Proteins. I. Weak and Strong Absorption of Bis(Dinitrophenyl)Lysine and Bis(Dinitrophenyl)Ornithine by Myosin

1967 ◽  
Vol 20 (5) ◽  
pp. 983
Author(s):  
RW Burley ◽  
WJH Jackson ◽  
Jean P Robertson
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Low Temperatures ◽  
High Ionic Strength ◽  
Total Absorption ◽  
Muscle Proteins ◽  
Skeletal Muscle Myosin ◽  
Skeletal Muscle Proteins ◽  
Sulphydryl Groups ◽  
Muscle Myosin

Below about 15�C in high ionic strength (0'5) phosphate buffer at neutral pH, the coloured compound bis(2,4.dinitrophenyl)-L-lysine (abbreviation bis-DNPlysine) was slowly but extensively absorbed from solution by rabbit skeletal muscle myosin. The absorption equations of Scatchard and of Klotz were not obeyed, thus suggesting that absorption did not involve independent sites. At higher temperatures, or if the myosin sulphydryl groups had been blocked with p-chloromercuribenzoate, absorption increased, often by as much as fivefold, and, moreover, a part of the absorbed bis-DNP-Iysine, probably corresponding to the "precipitation resistant" absorption reported previously, was strongly retained. Total absorption ofb~s-DNPlysine by myosin decreased slightly with increasing pH. At low temperatures bis-DNP-Iysine treatment induced the formation of small aggregates of myosin.

Proteomic Profiling of the Silkworm Skeletal Muscle Proteins during Larval−Pupal Metamorphosis

2007 ◽  
Vol 6 (6) ◽  
pp. 2295-2303 ◽  
Author(s):  
Pingbo Zhang ◽  
Yoichi Aso ◽  
Hiroyuki Jikuya ◽  
Takahiro Kusakabe ◽  
Jae Man Lee ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Proteins ◽  
Proteomic Profiling ◽  
Skeletal Muscle Proteins

scholarly journals Alcohol Affects the Skeletal Muscle Proteins, Titin and Nebulin in Male and Female Rats

2003 ◽  
Vol 133 (4) ◽  
pp. 1154-1157 ◽  
Author(s):  
R. J. Hunter ◽  
C. Neagoe ◽  
H. A. Järveläinen ◽  
C. R. Martin ◽  
K. O. Lindros ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Female Rats ◽  
Muscle Proteins ◽  
Male And Female ◽  
Male And Female Rats ◽  
Skeletal Muscle Proteins

The early expression of myofibrillar proteins in round postmitotic myoblasts of embryonic skeletal muscle

1990 ◽  
Vol 95 (1) ◽  
pp. 11-22
Author(s):  
N.J. Colley ◽  
K.T. Tokuyasu ◽  
S.J. Singer
Keyword(s):  
Skeletal Muscle ◽  
The Other ◽  
Myofibrillar Proteins ◽  
Muscle Proteins ◽  
Double Immunofluorescence ◽  
Light Microscopic Level ◽  
Early Expression ◽  
Specific Proteins ◽  
Muscle Cultures ◽  
Triton X

Previous reports on skeletal muscle myogenesis have shown that postmitotic spindle-shaped myoblasts express muscle-specific proteins, some of which are organized into nascent myofibrils. However, we show that, in skeletal muscle cultures derived from 12-day chick embryos, by 6 h after plating the predominant mononucleated cell type that expresses muscle-specific proteins is a round cell. These round myoblasts appear to precede spindle-shaped myoblasts in development, since the latter are more abundant in later cultures and contain larger amounts of muscle proteins and more highly organized myofibrils. By double immunofluorescence microscopy using antibodies specific for the muscle proteins titin, myosin heavy chain (MHC) and zeugmatin we find that 18 h after plating approximately 20% of the round myoblasts that are titin-positive are negative for myofibrillar MHC and zeugmatin. On the other hand, all spindle-shaped myocytes that are positive for titin are also positive for myofibrillar MHC and zeugmatin. These results suggest that titin expression precedes that of myofibrillar MHC and zeugmatin in the non-synchronized round myoblasts, and is consistent with earlier suggestions that titin may function as an initial organizer of myofibrillar proteins during myogenesis. Immunofluorescence data indicate that the earliest localization of the myofibrillar proteins titin, MHC, zeugmatin and alpha-actinin in the round myoblasts is surrounding the nucleus with no immunofluorescent labeling of the cytoplasm or near the plasma membrane. Furthermore, pairwise double immunofluorescence experiments show that these four myofibrillar proteins are all co-localized, at the light-microscopic level of resolution, in irregular patterns that may appear in either a punctate or a basket-like distribution. These labeling patterns around the nucleus are resistant to extraction with Triton X-100, suggesting that the proteins are associated in a stable array. These Triton X-100-resistant assemblies in round myoblasts appear to be composed solely of structural myofibrillar proteins, since the non-structural myofibrillar protein creatine kinase (CK) does not colocalize with the other myofibrillar proteins. These results indicate that in early myoblasts myofibrillar proteins form stable pre-myofibrillar assemblies surrounding the nucleus, and raise the possibility that these initial assemblies may play an organizing role during subsequent early stages of myofibrillogenesis.

ALTERED EXPRESSION OF SKELETAL MUSCLE PROTEINS DURING SEPSIS

Shock ◽  
1994 ◽  
Vol 2 (3) ◽  
pp. 171-178 ◽  
Author(s):  
Erik L. Owens ◽  
Christopher J. Lynch ◽  
Ken M. McCall ◽  
Nick D. Carter ◽  
Thomas C. Vary
Keyword(s):  
Skeletal Muscle ◽  
Muscle Proteins ◽  
Altered Expression ◽  
Skeletal Muscle Proteins

scholarly journals The binding of adenosine(5′)tetraphospho(5′)adenosine to calf thymus histones measured by non-equilibrium dialysis

1987 ◽  
Vol 246 (3) ◽  
pp. 681-686 ◽  
Author(s):  
G Just ◽  
E Holler
Keyword(s):  
Ionic Strength ◽  
Dissociation Constants ◽  
Equilibrium Dialysis ◽  
Physiological Saline ◽  
Histone H1 ◽  
The Other ◽  
Competition Assay ◽  
Calf Thymus ◽  
Non Equilibrium

Binding of adenosine(5′)tetraphospho(5′)adenosine (Ap4A) to histones of calf thymus was investigated by non-equilibrium dialysis. Histone H1 interacts with the dinucleotide via two strong sites and competes with Mg2+ ions. Intrinsic dissociation constants were 1.6 +/- 0.1 microM and 11 +/- 1 microM for zero and 0.4 mm-Mg2+ concentration respectively. Binding of poly(dT) and of other nucleotides to histone H1 was measured in an [3H]Ap4A-competition assay. The tendency to form complexes among nucleotides was highest for bisnucleoside tetraphosphates and decreased in the order poly(dT) greater than or equal to Ap4A approximately Gp4G greater than Ap4 much greater than Ap3A approximately Ap5A greater than or equal to ATP, GTP and dTTP. The co-ordination complex derived from Ap4A and cis-diammine-dichloroplatinum(II) was not reactive. The other histones of calf thymus also bound Ap4A with affinities decreasing in the order H4 approximately H3 greater than H1 greater than H2b greater than H2a. Ap4A stimulated the exchange of histone H1 between nucleosomes, but this effect was referred to ionic strength. It did not bind to assembled nucleosomes. Binding of Ap4A to histone H1 was decreased by salt (NaCl). At physiological saline concentration the value of the dissociation constant is commensurable with the value of the Ap4A concentration in the nucleus and thus indicative of complex-formation in vivo.

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