Phosphatase, acid, honey

Marz, L., Kuhne, C., and Michl, H. (1983). The glycoprotein nature of phospholipase As hyaluronidase and acid phosphatase from honey-bee venom. Tmdcan 21, 893— 896. 

A number of allergens from both honey bee and vespid venoms have been cloned and expressed by either Escherichia coli or baculovirus-infected insect cells (table 1) phospholipase Aj [20], hyaluronidase [21], acid phosphatase [13] and Api m6 [14] from honey bee venom, as well as antigen 5 [22], phospholipase A and hyaluronidase [23] from vespid venom, and dipeptidylpeptidases from both bee and Vespula venoms [15, 16]. Their reactivity with human-specific IgE antibodies to the respective allergens has been documented [11-16, 22, 23] and their specificity is superior... 

Grunwald T, Bockisch B, Spillner E, Ring J, Brede-horst R, Ollert M Molecular cloning and expression and expression in insect cells of honey bee venom allergen acid phosphatase (Api m3). J Allergy Clin Immunol 2006 117 848-854. 

The most prominent enzymes in honey are a-glucosidase(invertase or saccharase), a- and P-amylases (diastase), glucose oxidase, catalase and acid phosphatase. Average enzyme activities are presented in Table 19.14. Invertase and diastase activities, together with the hydroxymethyl furfural content, are of significance for assessing whether or not the honey was heated. 

Catalase in honey most probably originates from pollen which, unlike flower nectar, has a high activity of this enzyme. Similarly, honey acid phosphatase originates mainly from pollen, although some activity comes from flower nectars. 

Jacobson, R.S., and Hoffman, D.R., 1995, Honey-bee acid phosphatase is a member of the prostatic acid phosphatase family. J. Allergy Clin. Immunol. 95 372. (abstract)... 

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