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266 THE BLOOD.
the total blood. The same applies to the conjugated glucuronic acids,
which it seems, originate from the form-elements.
The blood-plasma and the serum, as well as the lymph also contain
enzymes of various kinds. According to Rohmann, Bial, Hamburger, 1
and others, diastases, which convert starch and glycogen into maltose or
isomaltose, as well as a maltase, are found in the blood. The diastase,
whose quantity is very variable in the blood of different animals, seems
at least in great part, to originate in the pancreas but can also come
from other organs and according to Haberlandt also from the leucocytes.2
Hanriot and others have detected, in the serum, lipases or esterases which
decompose butyrin and neutral fats and other esters. The occurrence
of butyrinases which split mono- as well as tributyrin has been recently
substantiated by Rona and Michaelis, while the property of this lipase
of splitting olein and other neutral fats is not generally acknowledged
(Arthus, Doyon and Morel 3
).
This lipolytic property, if it exists to the extent that Hanriot ascribes to
it, must not be confounded with the transformation of fat into unknown sub-
stances soluble in water, a phenomenon first observed by Connstein and Michae-
lis and further studied by Weigert. The occurrence of such a body is positively
denied by G. Mansfeld.4
Besides the above-mentioned enzymes and thrombin and the gly-
colytic enzymes that will be discussed later, several other enzymes have
been found in the blood-serum, namely, oxidases, catalases, proteolytic
enzymes, among which we must mention the polypepiide-splitting
enzymes studied by Abderhalden and collaborators,5
also rennin and
several antienzymes. We cannot enter into the discussion of these, nor
of the many not chemically characterized bodies which have been called
toxines and antitoxines, immune bodies, alexines, Iwmolysines, cytotoxines,
etc., and which have been discussed in Chapter I. The various enzymes
and antienzymes, and the above mentioned bodies are as a rule pre-
cipitated with the globulin, but differ among each other in that some are
’Rohmann: Rohmann and Hamburger, Ber. d. deutsch. chem. Gesellsch., 25
and 27; Pfliiger’s Arch., 52 and 60; Bial. Ueber das diast. Ferm., etc., Inaug.-Diss.
Breslau, 1892 (older literature). See also Pfliiger’s Arch., 52, 54, and 55; Wohlgemuth,
Bioch. Zeitschr., 21.
2
Wohlgemuth, 1. c; Moeckel and Rost, Zeitschr. f. physiol. Chem., 67; Clerk
and Loeper, Compt. Rend. soc. biol.. 66: Haberlandt, Pfliiger’s Arch.. 132.
3
Hanriot, Compt. Rend. soc. biol.. 48 and 54. Compt. Rend. 123 and 132; Rona,
and Michaelis, Bioch. Zeitschr., 31; Rona, ibid.. 33; Arthus, Journ. de Physiol, et
de Pathol., 4; Doyon and Morel, Compt. Rend. soc. biol., 54; Achard and Clerc
(Lipase in Disease), Compt. Rend., 129, and Arch. d. med. expe>., 14.
* Connstein and Michaelis, Pfliiger’s Arch., 65 and 69: Weigert, ibid., 82; Mansfeld,
Centralbl. f. Physiol, 21.
s
Zeitschr. f. physiol. Chem., 51, 53, 55.
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