Vines . — The Proteases of Plants (//). 1 6 1 
Germinating seeds: von Gorup-Besanez (’74), Green (’86, ’90), Neumeister (’94), 
Vines (Wheat-Germ ; ’03), Weis (’OS). 
Nepenthes : von Gorup-Besanez (’76), Vines ('77, '97, '98, '01), Clautriau (’00). 
Carica Papaya (papain) : Wurtz (’79), Martin (’84, ’85), Vines (’01, '03, ’05), 
Mendel and Underhill (’01), Emmerling (’02), 
Ficus Carica (Fig) : Hansen (’86, ’87), Mussi (’90), Vines (’02, ’05). 
Myxomycetes : Krukenberg (’79), Greenwood (’85, ’87). 
Bacteria: Bitter (’87), Lauder-Brunton and McFadyen (’89), Fermi (’90, ’91), 
Emmerling and Reiser (’02). 
Moulds ( Aspergillus , &c.) : Bourquelot (’93), Malfitano (’00), Butkewitsch (’02). 
Yeast ( Saccharomyces ) : Beyerinck (’97), Hahn and Geret (’98, ’00), Vines (’02, ’04). 
Basidiomycetous Fungi (Mushrooms, &c.): Hjort (’9 7), Vines (’03, ’04). 
Fruits: Ananas satiDus (Pine -apple) : Chittenden ('91, ’94), Vines (’02, ’03). 
Cucumis Melo var. utilissimus : Green (’92). 
Cucumis Melo (Melon) : Vines ( 03). 
Cucumis sa/ivus (Cucumber) : Vines (’03). 
Cucurhita Pepo var. ovifera (Vegetable Marrow) : Vines (’05). 
Asparagus officinalis (shoots) : Vines (’05). 
Phytolacca decandra (foliage-leaves) : Vines (’05). 
Bulbs: Hyacinthus orientalis and Tidipa sp. : Vines (’03, ’04). 
For the sake of completeness I may add that I have found evidence of 
the presence of erepsin in a great variety of plants : so many indeed that 
it may be assumed that this protease is present in some part, or most 
parts, of every plant at one stage or other of its development. In two 
cases (Yeast and Mushroom) I have satisfied myself of the simultaneous 
presence of erepsin and a fibrin-digesting protease (1). 
In conclusion, I would draw attention to the striking fact that the 
apparently universal distribution of erepsin in the tissues of plants that 
I have demonstrated, is paralleled by a similar distribution in the tissues of 
animals. This important discovery has recently been made by my friend 
and colleague, Dr. Vernon. His paper on the subject will shortly appear 
in the Journal of Physiology; in the meantime I have his permission 
to make use of the notes with which he has kindly supplied me. He has 
found that glycerin-extracts of the different organs of various animals, both 
vertebrate and invertebrate (e. g. frogs liver, pancreas, and ovary ; cat’s 
ovary, liver, lung, spleen and kidney ; rabbit’s kidney and liver ; pigeon’s 
kidney and liver ; eel’s kidney and liver ; sheep’s liver ; lobster’s muscle, 
liver, and kidney ; Anodon’s kidney, &c.), have no action on fibrin, but 
peptolyse Witte-peptone with various degrees of activity, tryptophane 
being always formed in the process. The protease is clearly erepsin. 
It acts more vigorously in dilute alkaline (o-i°/ o Na 2 C0 3 ) than in dilute acid 
(o-i °/ o acetic) liquids, differing in this respect from the erepsin of plants, 
which acts most vigorously, as I have shown, in liquids of the natural degree 
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