Abstract
Parvalbumins are characterized by their high solubility in water, low molecular weight of approximately 12 000, acidic isoelectric point, heat stability, high phenylalanine content relative to tyrosine and tryptophan and by their specific binding of 2 Ca’+-ions/molecule [I]. Parvalbumins have recently been found in muscle from higher vertebrates [2], but characterized in detail only in lower vertebrates [3-61 and rabbit muscle 12,781. No certain physiological function can be ascribed to them as yet. The myogen of chicken leg-muscle contains several acidic, low molecular weight components:
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