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January 1, 1964Biochemistry

Studies on UDPG-α-glucan Transglucosylase. V. Two Forms of the Enzyme in Dog Skeletal Muscle and Their Interconversion*

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Authors

MRM Rosell-PérezUniversitat de BarcelonaJLJoseph LarnerUniversity of Virginia Health System

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Implication

Biochemical analysis demonstrates two distinct forms of UDPG-α-glucan transglucosylase in canine skeletal muscle, indicating reversible interconversion mechanisms in glycogen synthesis.

Key Points

  • Determine the existence of distinct molecular forms of UDPG-α-glucan transglucosylase and characterize the mechanisms governing their interconversion in skeletal muscle tissue.
  • Extracted and fractionated UDPG-α-glucan transglucosylase from dog skeletal muscle preparations.
  • Assayed enzyme activity across various fractions to examine kinetic behavior and interconversion between forms.
  • Identified two distinct forms of UDPG-α-glucan transglucosylase in canine skeletal muscle displaying differing regulatory profiles.
  • Demonstrated enzymatic interconversion between the two states, establishing a dynamic biochemical switch for regulating muscle glycogen synthesis.

Cite This Study

Rosell-Pérez et al. (1964) studied this question.

synapsesocial.com/papers/6a6fc7898031ec7bb1dbf1adhttps://doi.org/10.1021/bi00889a014
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