If serum albumin from several animals, including humans,
at concentrations
greater than about 60 mg/mL is combined with an aqueous extract of
porcine or human pancreas, then massive amounts of microcrystals develop.
Both raw blood serum, as well as a range of concentrated, pure proteins,
when combined with the extract produced identical crystals. Morphologies
of crystals and their aggregates did, however, show some dependence
on the starting protein material. Crystals could be dissolved by boiling
in water and recrystallized. By X-ray diffraction we showed the crystals
to be l-tyrosine crystals, presumably a degradation product
of the starting proteins. Amino acid analysis, supported by mass spectrometry,
of even well washed crystals, however, consistently showed them to
be composed of 20% to 30% of other amino acids. An atomic force microscopy
investigation of the crystals revealed that the crystal surfaces were
persistently coated with spherical particles about 3 nm in diameter.
The particles are apparently micellar arrangements of oligopeptides.
Some implications of our results with regard the appearance of tyrosine
crystals in human tissues under pathological conditions, in tumors,
and in natural products such as foods are discussed.