scholarly journals The stereochemical course of phosphoryl transfer catalysed by Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinase with a chiral [16O,17O,18O]phosphate ester

1981 ◽  
Vol 199 (2) ◽  
pp. 427-432 ◽  
Author(s):  
R L Jarvest ◽  
G Lowe ◽  
B V L Potter
Keyword(s):  
Skeletal Muscle ◽  
Phosphorus Atom ◽  
Bacillus Stearothermophilus ◽  
Ternary Complexes ◽  
Rabbit Skeletal Muscle ◽  
Phosphoryl Group ◽  
Phosphate Ester ◽  
Phosphoryl Transfer ◽  
Enzyme Substrate

Bacillus stearothermophilus and rabbit skeletal-muscle phosphofructokinases catalyse the transfer of the chiral [16O,17O,18O]phosphoryl group from D-fructose 1[(S)-16O,17O,18O],6-bisphosphate to ADP with inversion of configuration at the phosphorus atom. D-Fructose 1[(S)-16O,17O,18O],-bisphosphate was synthesized in situ from sn-glycerol 3[(S)-16O,17O,18O]phosphate. The simplest interpretation of these results is that the phosphoryl group is transferred between substrates in the enzyme substrate ternary complexes by an ‘in-line’ mechanism.

Stereochemistry of phosphoryl transfer

1981 ◽  
Vol 293 (1063) ◽  
pp. 75-92 ◽  
Keyword(s):  
Absolute Configuration ◽  
Resonance Spectrum ◽  
Isotope Effects ◽  
Phosphate Esters ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Enzyme Substrate ◽  
Phosphate Monoesters ◽  
Line Transfer ◽  
General Method

A general method has been developed for the synthesis of chiral [ 16 O, 17 O, 18 O] phosphate monoesters of known absolute configuration. An analytic method for determining the absolute configuration of chiral phosphate esters has also been developed, which is based on the isotope effects of 17 O and 18 O at phosphorus in the 31 P nuclear magnetic resonance spectrum. These methods have shown that phosphoryl transfer catalysed by hexokinase, phosphofructokinase and pyruvate kinase occurs with inversion of configuration. This is most simply interpreted as an ‘in-line’ transfer of the phosphoryl group between substrates in the enzyme-substrate ternary complex.

scholarly journals Subcellular distribution of the 1,4-dihydropyridine receptor in rabbit skeletal muscle in situ: an immunofluorescence and immunocolloidal gold-labeling study.

1989 ◽  
Vol 109 (1) ◽  
pp. 135-147 ◽  
Author(s):  
A O Jorgensen ◽  
A C Shen ◽  
W Arnold ◽  
A T Leung ◽  
K P Campbell
Keyword(s):  
Skeletal Muscle ◽  
Subcellular Distribution ◽  
Staining Intensity ◽  
Dihydropyridine Receptor ◽  
Rabbit Skeletal Muscle ◽  
Beta Subunit ◽  
Type I ◽  
Tubular Membrane ◽  
Immunofluorescence Labeling

The subcellular distribution of the 1,4-dihydropyridine receptor was determined in rabbit skeletal muscle in situ by immunofluorescence and immunoelectron microscopy. Longitudinal and transverse cryosections (5-8 microns) of rabbit gracilis muscle were labeled with monoclonal antibodies specific against either the alpha 1-subunit (170,000-D polypeptide) or the beta-subunit (52,000-D polypeptide) of the 1,4-dihydropyridine receptor by immunofluorescence labeling. In longitudinal sections, specific labeling was present only near the interface between the A- and I-band regions of the sarcomeres. In transverse sections, specific labeling showed a hexagonal staining pattern within each myofiber however, the relative staining intensity of the type II (fast) fibers was judged to be three- to fourfold higher than that of the type I (slow) fibers. Specific immunofluorescence labeling of the sarcolemma was not observed in either longitudinal or transverse sections. These results are consistent with the idea that the alpha 1-subunit and the beta-subunit of the purified 1,4-dihydropyridine receptor are densely distributed in the transverse tubular membrane. Immunoelectron microscopical localization with a monoclonal antibody to the alpha 1-subunit of the 1,4-dihydropyridine receptor showed that the 1,4-dihydropyridine receptor is densely distributed in the transverse tubular membrane. Approximately half of these were distributed in close proximity to the junctional region between the transverse tubules and the terminal cisternae. Specific labeling was also present in discrete foci in the subsarcolemmal region of the myofibers. The size and the nonrandom distribution of these foci in the subsarcolemmal region support the possibility that they correspond to invaginations from the sarcolemma called caveolae. In conclusion, our results demonstrate that the 1,4-dihydropyridine receptor in skeletal muscle is localized to the transverse tubular membrane and discrete foci in the subsarcolemmal region, possibly caveolae but absent from the lateral portion of the sarcolemma.

scholarly journals Biogenesis of transverse tubules: immunocytochemical localization of a transverse tubular protein (TS28) and a sarcolemmal protein (SL50) in rabbit skeletal muscle developing in situ.

1990 ◽  
Vol 110 (4) ◽  
pp. 1187-1198 ◽  
Author(s):  
S Yuan ◽  
W Arnold ◽  
A O Jorgensen
Keyword(s):  
Skeletal Muscle ◽  
Subcellular Distribution ◽  
Developmental Stages ◽  
Rabbit Skeletal Muscle ◽  
Cell Periphery ◽  
Stages Of Development ◽  
Transverse Tubules ◽  
Ultrastructural Studies ◽  
Immunofluorescence Labeling

To study the biogenesis of transverse tubules, the temporal appearance and distribution of TS28 (a specific marker of transverse tubules absent from the sarcolemma in adult skeletal muscle; 28,000 Mr) and SL50 (specifically associated with the sarcolemma and absent from the region of the transverse tubules in adult rabbit skeletal muscle) (Jorgensen, A.O., W. Arnold, A. C.-Y. Shen, S. Yuan, M. Gaver, and K.P. Campbell. 1990. J. Cell Biol. 110:1173-1185) were determined in rabbit skeletal muscle developing in situ (day 17 of gestation to day 15 newborn) by indirect immunofluorescence labeling. The results presented show that the temporal appearance and subcellular distribution of TS28 is distinct from that of SL50 at the developmental stages examined. TS28 was first detected in some, but not all, multinucleated myotubes on day 17 of gestation. At this stage of development, SL50 and the Ca2(+)-ATPase of the sarcoplasmic reticulum were already present in all myotubes. TS28 first appeared in discrete foci mostly confined to the cell periphery of the myotubes. At subsequent stages of development (days 19-24 of gestation), TS28 was also found in shoft finger-like structures extending obliquely and transversely from the cell periphery towards the center of the myotubes. 1-2 d after birth, TS28 was observed in an anastomosing network composed of transversely oriented chickenwire-like networks extending throughout the cytoplasm and interconnected by longitudinally oriented fiber-like structures. As development proceeded, the transversely oriented network became increasingly dominant. By day 10 of postnatal development, the longitudinally oriented component of the tubular network was not regularly observed. At none of the developmental stages examined was TS28 observed to be uniformly distributed at the cell periphery. SL50, like TS28, first appeared in discrete foci at the cell periphery. However, shortly after its first appearance it appeared to be distributed along the entire cell periphery. Although the intensity of SL50 labeling increased with development, it remained confined to the sarcolemma and was absent from the interior regions of the myofibers, where transverse tubules were present at all subsequent developmental stages examined. Immunoblotting of cell extracts from skeletal muscle tissue at various stages of development showed that SL50 was first detected on day 24 of gestation, while TS28 was not detected until days 1-2 after birth. Comparison of these results with previous ultrastructural studies of the formation of transverse tubules supports the idea that the temporal appearance and subcellular distribution of TS28 correspond very closely to that of the distribution of forming transverse tubules in rabbit skeletal muscle developing in situ.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals The stereochemical course of yeast hexokinase-catalysed phosphoryl transfer by using adenosine 5′[γ(S)-16O,17O,18O]triphosphate as substrate

1981 ◽  
Vol 199 (1) ◽  
pp. 227-233 ◽  
Author(s):  
G Lowe ◽  
B V L Potter
Keyword(s):  
Ternary Complex ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Enzyme Substrate ◽  
Gamma S ◽  
Yeast Hexokinase

Adenosine 5′[gamma(S)-16O, 17O, 18O]triphosphate has been synthesized and used to determine the stereochemical course of phosphoryl transfer catalysed by yeast hexokinase. The chirality at phosphorus of the D-glucose 6-[16O,17O,18O]phosphate formed was analysed, after cyclization and methylation, by 31P n.m.r. spectroscopy. The phosphoryl transfer was found to occur with inversion of configuration, with a stereoselectivity in excess of 94%. The simplest interpretation of this result is that the phosphoryl group is transferred between substrates in the enzyme-substrate ternary complex by an ‘in line’ mechanism.

Phosphorylation of rabbit skeletal muscle myosin in situ

1985 ◽  
Vol 125 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Russell L. Moore ◽  
Michael E. Houston ◽  
James T. Stull ◽  
Gary A. Iwamoto
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

scholarly journals The stereochemical course of phosphoryl transfer catalysed by polynucleotide kinase (bacteriophage-T4-infected Escherichia coli B)

1981 ◽  
Vol 199 (1) ◽  
pp. 273-276 ◽  
Author(s):  
R L Jarvest ◽  
G Lowe
Keyword(s):  
Escherichia Coli ◽  
Phosphorus Atom ◽  
Bacteriophage T4 ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Polynucleotide Kinase ◽  
Gamma S ◽  
Escherichia Coli B

Polynucleotide kinase (bacteriophage-T4-infected Escherichia coli B) catalyses the transfer of the [gamma-16O,17O,18O]phosphoryl group from 5′[gamma(S)-16O,17O,18O]ATP to 3′-AMP with inversion of configuration at the phosphorus atom. The simplest interpretation of this observation is that the [gamma-16O,17O,18O]phosphoryl group is transferred directly from ATP to the co-substrate by an ‘in-line’ mechanism.

scholarly journals Biogenesis of transverse tubules and triads: immunolocalization of the 1,4-dihydropyridine receptor, TS28, and the ryanodine receptor in rabbit skeletal muscle developing in situ.

1991 ◽  
Vol 112 (2) ◽  
pp. 289-301 ◽  
Author(s):  
S H Yuan ◽  
W Arnold ◽  
A O Jorgensen
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Subcellular Distribution ◽  
De Novo ◽  
Outer Zone ◽  
Dihydropyridine Receptor ◽  
Rabbit Skeletal Muscle ◽  
Cell Periphery ◽  
T Tubules

Our previous immunofluorescence studies support the conclusion that the temporal appearance and subcellular distribution of TS28 (a marker of transverse (T) tubules and caveolae in adult skeletal muscle [Jorgensen, A. O., W. Arnold, A. C.-Y. Shen. S. Yuan, M. Gover, and K. P. Campbell, 1990, J. Cell Biol. 110:1173-1185]), correspond very closely to those of T-tubules forming de novo in developing rabbit skeletal muscle (Yuan, S., W. Arnold, and A. O. Jorgensen, 1990, J. Cell Biol. 110:1187-1198). To extend our morphological studies of the biogenesis of T-tubules and triads, the temporal appearance and subcellular distribution of the alpha 1-subunit of the 1,4-dihydropyridine receptor (a marker of the T-tubules and caveolae) was compared to (a) that of TS28; and (b) that of the ryanodine receptor (a marker of the junctional sarcoplasmic reticulum) in rabbit skeletal muscle cells developing in situ (day 19 of gestation to 10 d newborn) by double immunofluorescence labeling. The results presented show that the temporal appearance and relative subcellular distribution of the alpha 1-subunit of the 1,4-dihydropyridine receptor (alpha 1-DHPR) are distinct from those of TS28 at the onset of the biogenesis of T-tubules. Thus, in a particular developing myotube the alpha 1-DHPR appeared before TS28 (secondary myotubes; day 19-24 of gestation). Furthermore, the alpha 1-DHPR was distributed in discrete foci at the outer zone of the cytosol, while TS28 was confined to foci and rod-like structures at the cell periphery. As development proceeded (primary myotubes; day 24 of gestation) approximately 50% of the foci were positively labeled for both TS28 and the alpha 1-DHPR, while approximately 20 and 30% of the foci were uniquely labeled for TS28 and the alpha 1-DHPR, respectively. The foci labeled for both TS28 and the alpha 1-DHPR and the foci uniquely labeled for TS28 were generally confined to the cell periphery, while the foci uniquely labeled for the alpha 1-DHPR were mostly confined to the outer zone of the cytosol. 1-2 d after birth, TS28 was distributed in a chickenwire-like network throughout the cytosol, while the alpha 1-DHPR was confined to cytosolic foci. In contrast, the temporal appearance and subcellular distribution of the alpha 1-DHPR and the ryanodine receptor were very similar, if not identical, throughout all the stages of the de novo biogenesis of T-tubules and triads examined.(ABSTRACT TRUNCATED AT 400 WORDS)

Electron Probe Analysis of Muscle

1982 ◽  
Vol 40 ◽  
pp. 398-401
Author(s):  
A. V. Somlyo ◽  
H. Shuman ◽  
A. P. Somlyo
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Sarcoplasmic Reticulum ◽  
Resting State ◽  
Binding Sites ◽  
Electron Probe ◽  
Frog Skeletal Muscle ◽  
Electron Probe Analysis ◽  
Probe Analysis

Electron probe analysis of frozen dried cryosections of frog skeletal muscle, rabbit vascular smooth muscle and of isolated, hyperpermeab1 e rabbit cardiac myocytes has been used to determine the composition of the cytoplasm and organelles in the resting state as well as during contraction. The concentration of elements within the organelles reflects the permeabilities of the organelle membranes to the cytoplasmic ions as well as binding sites. The measurements of [Ca] in the sarcoplasmic reticulum (SR) and mitochondria at rest and during contraction, have direct bearing on their role as release and/or storage sites for Ca in situ.

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