Bromelain interactions with

Stem bromelain is able to interact with two or more sequential amino adds in a peptide substrate, demonstrated by using A -benzyloxycarbonyl-L-phenylalanyl-L-serine methyl ester [36]. A glutamic add residue in position P3 prevents cleavage of the susceptible peptide braid. The sequences containing negatively charged residues in position P3 and P4 remain intact [37]. 

Clinically important, potentially hazardous interactions with allopurinol, bromelain, chloramphenicol, demeclocydine, doxycydine, erythromycin, imipenem/cilastatin, methotrexate, minocycline, oxytetracycline, sulfonamides, tetracycline... 

Clinically important, potentially hazardous interactions with aldesleukin, bromelain, cimetidine, granulocyte colony-stimulating factor (GCSF)), metronidazole... 

Clinically important, potentially hazardous interactions with acitretin, aluminum hydroxide, amoxicillin, ampicillin, antacids, bacampicillin, betamethasone, bismuth, bromelain, calcium, carbenicillin, cholestyramine, doxacillin, corticosteroids, dairy products, dicloxacillin, didanosine, digoxin, food, glidazide, iron, isotretinoin, methicillin, methotrexate, methoxyflurane, mezlocillin, nafcillin, oxacillin, penicillins, piperacillin, retinoids, rocuronium, strontium ranelate, sucralfate, ticarcillin, vitamin A, zinc... 

A family of cysteine proteinase inhibitors different from the cystatin super-family was Isolated from pineapple stem acetone powder. These inhibitors have a Mr of about 5800 and are composed of a longer (41 amino acids) and a shorter (1L ammo acids) peptide chain connected with disulfide bonds [29]. The conserved sequence Gin- fal-Val-AJa-Gly of the cystatins is not present in these inhibitors, indicating a different mechanism of interaction. The bromelain inhibitor VI was found to share similar folding and disulfide band connectivities with the Bowman-Bilk trypsiu/chymatrypsm inhibitor from soybean [30,31]. Hie physiological role of these inhibitors remains undear. 

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