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December 15, 1992Biochemistry

Stereospecific reaction of muscle fiber proteins with the 5' or 6' isomer of (iodoacetamido)tetramethylrhodamine

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Population

Muscle fiber proteins (myosin subfragment 1 and actin)

Comparison

5' or 6' isomers oftetramethylrhodamine vs Comparison between 5'-IATR and 6'-IATR

Design

Preclinical

Authors

KAKatalin AjtaiMayo ClinicPIPredrag IlichLoras CollegeARAndras RinglerMayo Clinic

Discussion

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Implication

Isomer-specific IATR labeling differentiates muscle proteins; leaves open extension to human cardiac cross-bridge studies.

Structured PICO

P
Population
Muscle fiber proteins (myosin subfragment 1 and actin)
I
Intervention
5' or 6' isomers of (iodoacetamido)tetramethylrhodamine (IATR)
C
Comparator
Comparison between 5'-IATR and 6'-IATR
O
Outcome
Protein labeling characteristics, ATPase activity alteration, and fluorescence propertiessurrogate

The 5' and 6' isomers of IATR exhibit stereospecific labeling of muscle fiber proteins, with 5'-IATR specifically labeling myosin SH1 and indicating cross-bridge rotation, whereas 6'-IATR preferentially labels actin.

Cite This Study

Ajtai et al. (1992) studied this question.

synapsesocial.com/papers/6a714320c92390ac2d07ec8fhttps://doi.org/10.1021/bi00164a019
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Specificity and orientation of (iodoacetamido)proxyl spin-labeled myosin subfragment 1 decorating muscle fibers: localization of protein-bound spin labels using SDS-PAGE1990 · 15 citations
  2. 2Interaction of fluorescently labeled myosin subfragment 1 with nucleotides and actin1986 · 40 citations
  3. 3Myosin structure. Proximity measurements by fluorescence energy transfer1975 · 27 citations
  4. 4Fluctuations in polarized fluorescence: evidence that muscle cross bridges rotate repetitively during contraction.1979 · 93 citations
  5. 5Tryptic digestion as a probe of myosin S-1 conformation.1982 · 38 citations