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262 THE BLOOD.
(from horse-serum) was first performed by Gurber. It crystallizes
with difficulty from other blood-sera (Gruzewska). Even from horse-
serum only a portion, according to Robertson 1
not more than 40 per
cent, of the albumin can be obtained as crystals, and it is also pos-
sible that the amorphous albumin, which is precipitated by ammo-
nium sulphate with difficulty, represents two seralbumins (Maximo-
witsch). According to Gurber and Michel it would seem that the
crystalline seralbumin is also a mixture, but this is disproved by the obser-
tions of Schulz, Wichmann, and Krieger 2
. We know nothing as
to the behavior of the amorphous fraction of the seralbumin in this respect.
Because of the different coagulation temperatures, Halliburton claims
the existence of three different albumins in the blood-serum, a view
which has been disputed by several experimenters, and recently by
Hougardy. Oiv. the other hand, the earlier investigations of Kauder,
as well as the more recent work of Oppenheimer,3
seem to indicate a
non-unit nature of the seralbumins, but this question is still an open
one.
The crystalline seralbumin may perhaps be a combination with
sulphuric acid (K. Morner, Inagaki). The coagulated albumin obtained
from the aqueous solution of the crystals with the aid of alcohol has
almost the same elementary composition (Michel) as the amorphous
mixture of albumin prepared from horse-serum (Hammarsten and
K. Starke 4
). The average composition was C 53.06, H 6.98. N 15.99,
S 1.84 per cent. K. Morner, after the removal of the sulphuric acid
from crystalline albumin, found 1.73 per cent total sulphur, which prob-
ably exists only as cystine. Langstein 5
has been able to split off a nitrog-
enous carbohydrate (glucosamine) from crystalline seralbumin. The
quantity was so small that the question is still undecided whether or
not the carbohydrate was a contamination. The fact that Abder-
halden, Bergell, and Dorpinghaus 6
were able to prepare a seral-
bumin entirely free from carbohydrate and which did not respond to
Molisch’s very delicate reaction, seems to be decisive on this point.
The specific rotation of crystalline seralbumins from horse-serum was
found by Michel to be (a) D =—61 to 61.2°, and by Maximowitsch on
the contrary (o:) D = —47.47°.
1
Journ. of biol. Chem., 13.
2
In regard to the literature on the crystalline seralbumins, see Schulz, Die Kristal-
lisation von Eiweissstoffen, Jena, 1901; Maximowitsch, Maly’s Jahresber., 31, 35.
3
Halliburton, Journ. of Physiol., 5 and 7; Hougardy, Centralbl. f. Physiol., 15,
665; Oppenheimer, Verhandl. d. physiol. Gesellsch., Berlin, 1902.
4
Michel, Verhandl. d. phys-med. Gesellsch. zu Wiirzburg, 29, No. 3; K. Starke,.
Maly’s Jahresber., 11; K. Morner, 1. c; Inagaki, Biochem, Centralbl., 4, p. 515.
6
K. Morner, 1. c; Langstein, Hofmeister’s Beitrage, 1.
• Zeitschr. f. physiol. Chem., 41.
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