Biochem istry,
G ly c e ro l and p o ta s s iu m h y d r o x id e in t h e . m ic r o s c o p ic a l d e te ctio n o f b lo o d . K . Me i x n e r
(Deuts. Z. ges. gericlit. Med., 1927, 10, 253— 254;
Chem. Zeh.tr., 1927, ii, 1742).— A mixture of con
centrated aqueous potassium hydroxide and glycerol, or a glycerol solution of potassium hydroxide is preferred to aqueous potassium h yd roxid e; the formation of hsejmatin and htemochromogen takes place completely, but more slowly. The use of reducing agents for this purpose is objectionable.
A. A . El d r id g e. V alue o f b e n z id in e re a ctio n and the c lin ic a l s ig n ifica n ce of th e h se m a to p o rp h y rin te st in faeces. D. E. Sc hou t e n (Ned. miaandschr. geneesk., 1926, 13, 651— 668; Chem. Zentr., 1927, ii, 963).—
The pigment of the blood is partly or completely converted in the intestinal canal into hiematopor- phyrin; spectroscopic detection of the porphyrin is preferred. The test is not less sensitive than the benzidine reaction. A. A. El d r id g e.
E ffe ct o f p o s tu r e o n th e c o m p o s it io n and v o lu m e of b lo o d in m a n . W . 0 . Th o m p so n, P. K . Thom pson, and M. E. Da i l e y (Proc. Nat. Acad.
Sci., 1928,14, 94— 98).— In the standing-still position there occurs a net loss of approximately protein-free fluid from the blood. This seems to be due to an increase in capillary pressure. The loss amounts to about 1 1% of the total plasma volume, and is pro
bably greatest in the lower extremities.
W . E. Do w n e y. O rig in of th e p ig m e n t o f C h iro n o m n s larvae.
M. Comas (Compt. rend. Soc. Biol., 1927, 96, 866— 868; Chem. Zentr., 1927, ii, 100).— Hamioglobin in Chironomus larvae does not arise from ingestion of chlorophyll, but is hereditary. It is associated with a green pigment similar in its properties to biliverdin.
A . A. El d r id g e. C oagu la tion of h aem oglob in in p re s e n ce o f o rg a n ic su bstan ces. B. Jir g e n s o n s (Biochem. Z., 1928, 193, 109— 121).— The coagulation of haemo
globin with potassium chloride and magnesium chloride is sensitised by the presence of small amounts of capillary-active substances having small dielectric constants (ether, chloroform, amyl and i'sobutyl alcohols, acetone, methyluretliane), whilst in larger concentrations these substances m ay act either as sensitisers if the salt concentration is small, or as stabilisers if it is large. Some capillary-inactive substances (mannitol and dextrose) have a slight stabilising action (cf. A ., 1927, 512, 624).
P. W . Cl u t t e r b u c k. Amino-acids in blood of insects. M. D u v a l, P. P o r t i e r , and A. C o u r to is (Compt. rend., 1928, 186, 652— 653).— Amino-acids have been determined b y the Sorensen titration method in the blood of insects, in the chrysalid, larval, and fully-grown states. The value is high in each case, and par
ticularly in the chrysalis. W . K . S l a t e r . Blood-creatinine. O. H. G a e b l e r and A. K . K e l t c h (J. Biol. Chem., 1928, 76, 337— 359).—
Addition of a 10% solution of phosphotungstic acid,
saturated with picric acid, to a saturated picric acid solution containing creatinine causes precipitation of the latter; the precipitate can be decomposed with a mixture of alcohol and ether and the creatinine re-precipitated by addition of picric acid to the filtrate. Picric acid is removed b y shaking the pre
cipitate with dilute sulphuric acid and ether, the creatinine is re-precipitated with basic lead acetate, recovered with hydrogen sulphide in tho usual manner, and finally isolated as potassium creatinine picrate; in order to obtain the maximum yield of the latter it is important to have the correct con centration of potassium in tho solution. The above method has been applied to the isolation of creatinine from blood which has been freed from protein by treatment with picric acid. Treatment of such protein-free blood-filtrates with kaolin removes the creatinine but leaves in solution other substances which give the Jaffe reaction and also accumulate in those pathological conditions which lead to reten
tion of creatinine. Creatinine m ay also be separated from blood-filtrates by treatment with L loyd’s reagent, and decom position of the precipitate by means of lead hydroxide. C. R . Ha r in g t o n.
D e te rm in a tio n o f c h o le s te ro l in s m a ll a m o u n ts of b lo o d . S. M. Lin g (J. Biol. Chem., 1928, 76, 361— 365).— Blood is dried on iiltcr-paper and extracted for 40 mm. with chloroform in a special apparatus; cholesterol in the extract is determined colorimetrically. C. R . Ha r in g t o n.
D e te rm in a tio n o f d ih y d ro x y a ce to n e in b lo o d a n d u rin e. W . S. McCl e l l a n (J. Biol. Chem., 1928, 76, 481— 486).— The utility of the method of Campbell (A., 1926, 443) for the determination of dihydroxyacetone in blood is confirm ed; the method can be applied to urine, after preliminary removal of phosphates. C. R . Ha r in g t o n.
M e th y lg ly o x a l as in te rm e d ia te p r o d u c t in g ly c o ly s is in b lo o d . H . K . Ba r r e n s c h e e n (Bio
chem. Z., 1928, 193, 105— 10S).— The formation of methylglyoxal during glycolysis in blood is detected b y addition of semicarbazide with isolation and identification of methylglyoxal disemicarbazone.
P. W . Cl u t t e r b u c k. G ly c o ly s is o f d e x tr o s e and lsevulose in the b lo o d o f n o r m a l and d ia b e tic d o g s . E . Tu r g a t t i
(Rev. Soc. Argentina Biol., 1927, 3, 716— 720);
— Venous blood from dogs was incubated for 6 lirs., alone, and with the addition of dextrose or lsevulose. The greatest amount of glycolysis occurred in blood of low blood-sugar level, and vice versa.
Glycolysis was retarded considerably by the addition of dextrose and moderately by the addition of lsevul
ose. Glycolysis was slower in the blood o f dogs from which the pancreas had been removed, and was retarded or even inhibited by addition of dextrose, but the addition of lsevulose had, on the whole, little effect. . It is suggested that liyperglycscmia can be considered not only as a sym ptom , but also as itself a cause of disturbance. R- K- Ca l l o w.
438 BIRTISH CHEMICAL ABSTRACTS.— A .
“ P r o t e i n ’ ’-b lo o d -s u g a r . E. J. Big w o o d and A. Wu il l o t (Compt. rend. Soc. Biol., 1927, 9 7 , 186— 187 ; Chem. Zentr., 1927, ii, 1162).— Hydrolysis of plasma-protein yields a small fraction of a reducible and fermentable substance, having a reducing power about 6% of that of the sugar-free hydrolysatc; the ratio of protein to the substance is about 1 : 0-0044.
A. A. El d r id g e. R e d u c in g and fe rm e n ta b le su b sta n ce s in c o m b in a tio n w ith p ro te in s o f the b lo o d -p la s m a . E. J. Big w o o d and A . Wu il l o t (Compt. rend. Soc.
Biol., 1927, 97, 187— 191; Chem. Zentr., 1927, ii, 1162— 1163; cf. preceding abstract).— Pure con
stituents of the blood-serum were submitted to hydrolysis. Proteins give by acid hydrolysis 7-4%
of reducing substance expressed as dextrose and calculated on the original quantity of sheep blood- proteins; the fermentable fraction is only 0-S—1-2% , and is ascribed to traces of nucleoproteins.
A. A. El d r id g e. P re s e n ce of tw o re d u cin g ca rb o h y d ra te s in b lo o d . G. Fo nti-isand L. Th iv o l l e (Compt. rend.
Soc. Biol., 1927, 96, 994— 996; Chem. Zentr., 1927, ii, 449).— The use of mercuric nitrate and of tungstic acid (the former, but not the latter, precipitating creatinine and uric acid) indicates the presence in blood, in addition to that of “ glucose,” of an ethereal component the reducing power of which is unchanged by hydrolysis. The amount is not increased by muscular work or insulin. A . A. El d r id g e.
D istrib u tio n o f the ca rb o h y d ra te re d u cin g su b sta n ce s b etw een p la s m a and b lo o d -c o r - p u scle s. G. FoNTjfcs and L. Th iv o l l e (Compt.
rend. Soc. Biol., 1927, 96, 997— 99S; Chem. Zentr., 1927, ii, 449).— Hirudin does not affect the natural distribution of reducing carbohydrates in the cor
puscles ; other anticoagulants affect the plasma and corpuscles in the same sense. A. A. El d r id g e.
D e te rm in a tio n o f b lo o d -s u g a r . II. S. R . Be n e d ic t (J. Biol. Chem., 1928, 7 6 , 457— 470).—
Evidence was obtained of the presence in protein- free blood filtrates of substances which affect the dissociation of the com plex copper salt, in the solu
tions usually employed for the determination of blood-sugar, rendering it more easily reduced by dextrose; this effect has been overcome by the addition of alanine to a new reagent of the Fehling type. The new reagent gives results for the blood- sugar about 22 m g.% lower than the reagent of Folin and Svcdberg (A., 1926, 1282); further, dextrose added to protein-free filtrates of blood which have been subjected to yeast fermentation can be quantit
atively determined by the new reagent, which there
fore appears not to be affected by the non-dextrose reducing substances present in such filtrates. The work of Som ogyi (A., 1927, 1214) is criticised on the ground that insufficient time was allowed for ferm entation; good results are obtained b y diluting blood with a suspension of washed yeast and keeping the mixture for 15 min. before precipitation with tungstic acid, C. R . H a rin g to n .
M icr o -d e te r m in a tio n o f b lo o d -s u g a r . H . Cit r o n (Deutsch. med. W och., 1927, 53, 1216—
1217; Chem. Zentr., 1927, ii, 1598).— The H agedorn- Jensen method is improved. A. A. El d r id g e.
S e r u m -c a lc iu m . I. O ra l a d m in is tra tio n . J. C. Ho y l e (J. Pharm. Exp. Ther., 1928, 3 2 , 309—
320).— N o definite differences in the normal serum- calcium content of male and female rabbits have been detected, but a seasonal variation occurs. Loss of blood equivalent to about one fifth of the body- weiglit causes a fall in the serum-calcium of approxim
ately 14-%. Administration by mouth of single or repeated doses of 1 g. of calcium carbonate per kg.
body-wcight causes an increase of serum-calcium up to 16% which, when allowance is made for effect of hannorrhage, is equal to an increase of 20— 25% . B y administration of 2 g. of calcium carbonate per day a permanent increase of serum-calcium of 5— 15%
has been obtained. Single doses of calcium lactate (3 g. per kg. body-wcight) cause an increase in serum- calcium of 15— 22% , whilst repeated daily doses of 6 g. of the salt cause a maximum increase of only 5 % , or 12% if allowance be made for the effects of repeated bleeding. W . 0 . Ke r m a c k.
R e p la ce m e n t o f the s e r u m -c a lc iu m and th y r o id g la n d in ra b b its a fter in tra ven ou s in je ctio n s o f oxa la te. H. W . C. Vin e s (Endocrinol., 1927, 1 1, 290— 296).— The speed of replacement of calcium, which has been removed from the blood following the intravenous injection of ammonium oxalate, was determined. Ch e m ic a l Ab st r a c t s.
B lo o d -p h o s p h o r u s in h ealth and d isease. I.
D istrib u tio n o f p h o s p h o ru s in h u m a n b lo o d in h ealth . H . D . Ka y and F . B. By r o m (Brit. J. E xp.
Path., 1927, 8, 240— 253).— The distribution of phosphorus in venous blood is fairly constant; the ester phosphorus is greater, and the portion thereof hydrolysable by phosphatase is less, in men than in women. After a meal there is a slight diminution in inorganic phosphorus, a diminution in phosphoric ester hydrolysable by phosphatase, and a corre
sponding increase in the ester fraction resistant to enzyme hydrolysis;' there is also possibly a slight rise in lipin-phosphorus. The phosphorus index (mg. of ester phosphorus in 100 c.c. of red cells) is a more stable constant than the p a of the blood.
Ch e m ic a l Ab s t r a c t s. U se of the q u in h y d ro n e e le ctro d e fo r the d e te rm in a tio n o f the ]>n o f w h o le b lo o d and s e ru m . J. Ge w e c k e (Biochem. Z., 1928, 1 9 3 , 181— 186).— The experiments of F . Schmidt (Z.
Immun. exp. Ther., 1926,4 6 ,386) were repeated using rabbit’s in place of guinea-pig’s blood, but the results were not consistent and often very different from those obtained b y the hydrogen electrode. W ith inactivated human serum the initial potential was highest and quickly fell, and the results again differed from those obtained by the hydrogen electrode.
P. W . Cl u t t e r b u c k. D e te rm in a tio n of p a of b lo o d . I. A c c u r a c y o f q u in h y d ro n e e le ctr o d e fo r d e te rm in in g p B o f b lo o d -p la s m a o r se ru m . G. E. Cu l l e n and I. P.
Ea r l e. II. C o m p a r is o n of c o lo r im e t r ic m e th o d w ith h y d ro g e n a n d q u in h y d ro n e e le ctro d e s.
I. P. Ea r l e and G. E. Cu l l e n (J. Biol. Chem., 1928, 7 6 , 565— 581, 583— 590).— I. A modified technique
BIOCHEMISTRY. 439
for the use of the quinhydrone electrode (cf. Cullen and Biilmann, A., 1925, i, 1201) is described, by the employment of which reproducible results for the p a of normal blood-plasma or -serum m ay be obtained, these results being always 0'06 p B more acid than the corresponding figures obtained with the hydrogen electrode.
II. Figures obtained for the p B of normal diluted human blood-serum b y the colorimetric method of Cullen (A., 1922, ii, 072) were 7-41— 7-50, and were 0-14 p a more alkaline than those obtained with the quinhydrone electrode. C. R . Ha r in g t o n.
C alcu lation of ce ll v o lu m e ch a n g e s as a fun ction of p B. D. B. Dill (J. Biol. Chem., 1928, 76, 543— 545).— B y mathematical extension of the calculations of Van Slyke, W u, and McLean (A., 1923, i, 1249) a relationship is developed between the relative volume of the red blood-corpusclcs and thep B of the serum. C. R . H a r in g t o n .
E ffe ct of c a r b o n d io x id e e q u ilib ra tio n on surface ten sion o f b lo o d -s e r u m . J. M. Jo h l in
(J. Biol. Chem., 1928, 76, 559— 564).— Neither the absolute magnitude of the surface tension of blood- serum nor the change in surface tension with time is significantly affected by equilibration with varying tensions of carbon dioxide. C. R . Ha r in g t o n.
H aem oclastic ch a n g e s in v itro f r o m agen ts ca u sin g a n a p h y la ctoid re a ctio n s . P. J. Ha n z l ik, F. De Ed s, L . W . Em p e y, and W . H . Far r
(J. Pharm. Exp. Then, 1928, 32, 273— 294).—
Various anaphylactoid reagents, copper sulphate, arsphenamine, peptone, acacia, agar, and toxified serum added in vitro to oxalated blood-plasma or serum cause a decrease in surface tension and an increase in the albumin-globulin ratio. Albumin, peptone, and agar increase the viscosity of blood- serum, acacia and gelatin increase the rate of sedi
mentation of blood-corpuscles suspended in plasma.
The fragility of the corpuscles is decreased by acacia and gelatin and increased by arsphenamine and copper sulphate. The results are considered to support the view that anaphylactoid changes are of the nature of a disturbance in the equilibrium of the body colloids. W . 0 . Ke r jia c k.
V a ria tion s in the c o a g u la b ility o f th e b lo o d n o rm a lly and after in g e stio n o f fo o d . C. A.
Mil l s and H . Ne c h e l e s. R e la tio n o f b lo o d co a g u la b ility to b o d y m e ta b o lis m and to the s p e cific d yn am ic a ction o f fo o d . H . Ne c h e l e s
and C. A. Mills (Chinese J. Physiol., 1928, 2 ,19— 23, 25— 32).— The coagulation time of blood is decreased after a meal containing protein, but not after one containing only carbohydrate or fat. It is decreased also after administration of glycine, which, like proteins, has a marked specific dynamic action. The decrease in coagulation time appears to be related, not directly to the increase of metabolism which occurs after a meal, but rather to the presence in the blood
stream of substances which exert specific dynamic
action. W . 0 . Ke r m a c k.
A ctio n of so lu b le iro n salts on co a g u la tio n o f b lo o d . P. Bo r d e t (Compt. rend. Soe. Biol., 1927, 96, 1061— 1063; Chem. Zentr., 1927, ii, 450).—
Ferrous sulphate and chloride, aluminium sulphate*
and chrome alum hinder the coagulation of blood owing to interaction with the blood constituents.
A . A. El d r id g e. C h e m is tr y o f s p e c ific h æ m a g g lu tin a tio n . A . Ko n ik o v (¿urn. eksp. biol. med., 1926, 128— 145;
Chem. Zentr., 1927, ii, 1046).— The erythrocytes can be regarded as an amphoteric protein of isoelectric point p n 5. Probably only between p n 6 and 9 arc the stroma and agglutinin oppositely charged. The presence of electrolyte is necessary in the first phase of hæmagglutination; the action of the salt is ex
pressed by the scheme stroma— Na— Cl— agglutinin, I____________________I in which auxiliary valencies function. The subject is discussed from this point of view. A. A. El d r id g e.
R a p id p re p a r a tio n o f cry s ta llin e e g g -a lb u m in . W . La Rosa (Chemist-Analyst, 1927, 16, No. 2, 3).—
The whites of fresh eggs are beaten well and mixed with an equal volume of saturated ammonium sulphate solution. After 15 hrs. the liquid is centri
fuged and the clear supernatant liquid is siphoned off. Acetic acid (10% ) is then added, with stirring, until a permanent turbidity appears, an additional 1 e.c. for each 100 c.c. of liquid being finally added.
Ch e m ic a l Ab st r a c t s. P h y s io lo g y o f th e foetus. T. Su g a n o (Kinki Fuji. Gak. Zassi, 1926, 9, 97— 100; Chem. Zentr., 1927, ii, 945).— Pepsin appears in the foetus at the fifth or sixth month. A. A. El d r id g e.
O x id is in g s u b sta n ce s in a n im a l ce lls. W . Lo ele (Arch. path. Anat. Physiol., 1926, 261, 484—
502; Chem. Zentr., 1927, ii, 943).
M ic r o c h e m is tr y o f the ce ll. I. C h ro m a tin co n te n t o f n o r m a l a n d m a lig n a n t ce lls. R . J.
Lu d f o r d (Proc. R oy. Soe., 1927, B , 102, 397— 406).
— The chromatin content of various normal and abnormal animal cells has been investigated by means of Feulgen’s “ nucleal ” reaction ” During oogenesis in the rat and in the mouse there is no increase in the chromatin content of the nuclei, and when formation of the chromosomes takes place no chromatin is extruded into the cytoplasm ; the heads of the spermatozoa of the rat and the mouse contain chrom
atin. Experiments on the nuclei of gland cells before and after secretory activity indicate no appre
ciable diminution in chromatin content. There is no correlation between the amount of chromatin in the nuclei of tumour-cells and the rate of growth of the tumour ; the nuclear extrusions occurring in certain tumours do not consist of chromatin.
E. A. Lu n t. O x id is in g a n d r e d u c in g p o w e r s o f m it o ch o n d ria . P. Jo y e t-Laverc.n e (Compt. rend., 1928,186, 471— 473).— Histological studies have been made on the effect of certain comparatively non
toxic substances which become coloured on oxidation, e.g., quinol, “ m etol,” pyrogallol, and of aqueous solutions of gold chloride and of silver nitrate on fresh liver cells, and are held to indicate the oxidising and reducing properties of the chondriosomc system.
E. A. Lu n t. S p e c t r o p b o to m e tr ic stu d ies o f the tw o c o m p o n e n ts o f try p a n -b lu e . (A d s o rp tio n th e o ry of
440 BRITISH CHEMICAL ABSTRACTS.— A .
v ita l sta in in g .) N. O k u n e f f (Biochem. Z., 1928, 193, 70— 84).— Aqueous solutions of trypan-blue possess a definite absorption constant (max. 0-911) and a definite absorption maximum (580— 590 ¡41).
The absorption constant is independent of the con
centration within certain limits (1/5000— 1/100,000), but differs with the different commercial samples of the dye. W hen strips of filter-paper arc dipped in dilute solutions of the dye, the solution gradually becomes red and the paper blue, the absorption constant then showing a progressive decrease and the absorption maximum a displacement to the left.
The blue component is adsorbed much more firmly than the red. Addition of gelatin, protein, or plasma- colloids increases the adsorption constant and dis
places the absorption maximum to the right. The fate of the two components in the organism is there
fore conditioned, not only b y tlicir different diffusi- bilities, but also by their different adsorbabilities.
P. W . Cl u t t e r b u c k. M ic r o c h e m ic a l d e te ctio n o f p o ta s s iu m and c a lc iu m in h is to lo g ic a l s e ctio n s. W . Ja c o b i and W . Ke u s c h e r (Arch. Psych. Ncrv., 1927, 79, 323—
326; Chem. Zentr., 1927, ii, 1985— 1986).— The tests depend, respectively, on the formation of potassium chloroplatinate and calcium sulphate.
A. A . El d r id g e. C h e m ica l c o m p o s it io n a n d h is to lo g ic a l s tr u c tu re o f n o r m a l and a tro p h ie d m u s cle . T. Ca h n
(Ann. physiol, physicochim. biol., 1926, 2, 646— 681;
Chem. Zentr., 1927, ii, 846— 847).— A critical review.
C o m p o s itio n o f h u m a n e p id e rm is . Y . J o no (J. Biophys., 1927, 2, xlviii).— Human epidermis contained water 20% , ash 1-5% (the silica content being high; sulphur content of ash 0-78% ), fat 2 % . Hydrolysis of the protein yielded tyrosine, leucine, alanine, valine, isoleucine, proline, glutamic acid, arginine, and lysine. Ch e m ic a l Ab st r a c t s.
F e rm e n ts of h u m a n sk in . N . Me l c ze r (Der
matol. Z., 1926, 49, 252— 261; Chem. Zentr., 1927, ii, 945).— Diastase, phenolase, catalase, peroxidase, and glycolytic ferment are present in human sk in ; .lipase is produced by the epidermal cells. In fatal pulmonary or peritoneal tuberculosis the skin lipase is practically or completely absent.
A. A. El d r id g e. O rg a n ic con ten t o f h u m a n e n a m el. C. Sp r a w- son and F. W . Bu r y (Proc. R oy. Soc., 1927, B , 102, 419— 426).— The protein content of human enamel calculated from the nitrogen and the carbon contents of enamel is, respectively, 0-15% and 0 -2 1 % ; it is suggested that the discrepancy in these results is due to the contamination of the enamel with carbon from the steel used in filing the enamel from the tooth. The organic content of enamel is independent of the dentition or the age of the tooth.
E. A. Lu n t. D e te rm in a tio n o f glu tath ion e. A. Bl a n c h e- TifiRE and L. Melon (Compt. rend. Soc. Biol., 1927, 97, 242— 244; Chem. Zentr., 1927, ii, 1495).—
Tunnicliffe’ s method is preferred to that of Thompson and Voegtlin. The lower limits of sensitiveness are for cysteine, 200 mg. per litre, and for reduced glut
athione 125 mg. per litre. A. A. El d r id g e.
O s m o tic co n ce n tra tio n o f se cr e tio n s . J.
St r a u b and L. Soep (Arch. Neerland. Physiol., 1928.
12, 346— 367).— A series of analyses o f secretions and sera before and after dialysis, with an interpretation of the results in the light of modern theories.
W . Ro b s o n. B a c te ria l g r o w th as a fa c to r in th e d e p o s itio n of c a lc iu m f r o m saliv a. W . A . Pe a b o d y, I. C.
Ha l l, and R . C. Le w is (Dental Cosmos, 1927, 69, 10S7).— Direct precipitation of calcium in centri
fuged saliva determines at least 93% of the total calcium. Incubation of raw saliva with or without excess of fermentable carbohydrate produces, re
spectively, an acid reaction with an increase of soluble calcium, or an alkaline reaction with a decrease of soluble calcium. Ch e m ic a l Abst r a c t s.
C o m p o s itio n o f sy n o v ia l flu id . F . A . Cajo r i and R . Pe m b e r t o n (J. Biol. Chem., 1928, 76, 471— 4S0).— The concentrations of the non-protein
C o m p o s itio n o f sy n o v ia l flu id . F . A . Cajo r i and R . Pe m b e r t o n (J. Biol. Chem., 1928, 76, 471— 4S0).— The concentrations of the non-protein