Abstract
Acid trimetaphosphatase has been used as a cytochemical marker for lysosomes in mammalian tissues. Application of the same technique, which employs glutaraldehyde as a fixative, to soybean hypocotyl tissues resulted in staining mainly of nuclei. Sodium fluoride, an effective phosphatase inhibitor, did not prevent but intensified nuclear staining. Nuclei were not stained in formaldehyde-fixed tissues; lead deposits occurred in vacuoles, but ultrastructural preservation was poor and the cytochemical response was inconsistent. Acid trimetaphosphatase activity was demonstrated readily in vitro in protein extracts of soybean tissues, and was strongly inhibited by sodium fluoride. Activity was much reduced in extracts from glutaraldehyde-fixed tissues but not in extracts from formaldehyde-fixed tissues in which it was similar to that in controls. It is concluded that nuclear staining for acid trimetaphosphatase is an artifact of glutaraldehyde fixation, and it is suggested that reports of nuclear staining of acid phosphatases in plant tissues should be interpreted with caution.
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