A n im al life in syn th etic m ix tu r e s of n itrogen and oxygen . J . W . He r s h e y (Trans. K ansas Acad.
Sei., 1930, 33, 133— 136).— Sm all anim als died in gas containing 21% 0 2 a n d 69% N 2 b u t lived norm ally w hen th e 0 2 c o n ten t w as 25— 60% .
Ch e m i c a l Ab s t r a c t s.
M icro-d eterm in ation of oxygen and carbon dioxid e in blood . H . W . Mo o k (Biochem. Z., 1931, 242, 338— 347).— A solution of 0-5 g. of K 3F e(C K 6) in 100 c.c. of H 20 m ade alkaline w ith 1 c.c. of 25%
N H 3 absorbs all th e C 0 2 from th e gas lib e ra te d from blood on ev acu atio n an d leaves all th e 0 2 free. T he
B IO C H E M IS T R Y . 7 3
ap p lica tio n of th e a p p a ra tu s p reviously described (A., 1930, 1201) to th e d e te rm in a tio n of 0 2 an d C 0 2 in 50— 70 c.c. of blood is described. A p rocedure for w ithdraw ing th e blood from th e finger w ith o u t p e r
m ittin g gaseous exchanges to occur is also described.
W . McCa r t n e y.
Copper and b lood form ation . Vo n Li n d e n
(Med. W elt, 1931, 5, 629; Chem. Z e n tr., 1931, i, 3254).— Cu p lay s a n im p o rta n t p a r t in th e living organism and, in c e rta in conditions, h as th e ra p e u tic
val. A. A. El d r i d g e.
A ction of phenylhydrazine and phenylhydr- oxylam in e on tb e m e ta b o lism of red b lo o d -c ells.
D eterm in ation of m e ta b o lism of red b lood -cells.
0 . Wa r b u r g, F . Ku b o w i t z, a n d W . Ch r i s t i a n
(Biochem. Z., 1931, 242, 170— 205).— Methsemo- globin, p roduced in e ry th ro c y tes b y am y l n itrite , oxidises c a rb o h y d rate, becom es reduced to h e m o globin, a n d on shak in g w ith 0 2 gives o x y hem oglobin.
T h e a c tio n is n o t c a ta ly tic b u t stoicheiom ctric. T he m etluem oglobin o b tain ed b y tre a tm e n t of ery th ro c y te s w ith N H P h -O H is reduced an aerobically to h e m o globin a n d th e so lution on ox y g en atin g gives only h em o g lo b in . If, how ever, th e m e th e m o g lo b in re a c ts in th e cell aerobically w ith carb o h y d ra te, reo x id atio n gives b ack m etluem oglobin, th e re a c tio n being c a ta ly tic . T he re sp iratio n of r a b b it’s e ry th ro c y te s w ith N H P h -O H is 20 tim es norm al. N H P h -N H 2 a d d ed to th e re d cells in vitro colours th e m brow n an d re sp ira tio n is g re a tly increased. N H P h -N H 2 d estro y s haemoglobin, lib eratin g ham iin a n d d e n a tu rin g globin.
T he lib e ra te d haemin oxidises oxy- to m et-luem oglobin a n d th e la tte r oxidises ca rb o h y d ra te. Haem, so form ed, is th e n reoxidised b y 0 2 to haemin a n d haemo
globin to oxyhaemoglobin, th u s reg en eratin g th e o riginal system . W h en N H P h -N H 2 is in jecte d in to ra b b its, th e re sp iratio n of red cells increases b y 20 to 40 tim es. T hese cells a re n o t brow n as in experim ents in vitro a n d th e y c o n tain d e n a tu re d globin b u t no free haemin, th is hav in g been ex creted or destroyed.
P . W . Cl u t t e r b u c k.
P h y sic a l ch em istry of p ro tein s. V III. S o lu b ility of haem oglobin in concentrated sa lt so lu tio n s. S a ltin g ou t of p rotein s. IX . E ffect of electro lytes on so lu b ility of haem oglobin in so lu tio n s of v ary in g h yd rogen -ion activity. C om p arab le b ehaviour of casein ogen . A . A . Gr e e n
(J. Biol. Chem., 1931, 93, 495— 516, 517— 542).—
V I I I . T h e solubilities of carboxy- an d oxy-haemo
globin in conc. K 2H P 0 4 buffers, a n d of th e fo rm er in N a2S 0 4, (N H 4)2S 0 4, M gS 04, a n d N a citra te , hav e been d eterm in ed b y e q u ilib ratio n a n d conform , a t const, te m p . a n d p H, to th e e q u a tio n log S —$—K 's[i, w here u.
is th e ionic stre n g th , p d epends on th e p ro te in a n d p a. Increase of te m p , from 0° to 25° decreases th e so lu b ility of carboxyhicm oglobin in p h o sp h a te solutions tenfold. K '„ w hich is in d e p e n d en t of tem p , a n d p H, varies w ith th e electrolyte, decreasing in th e o rd er K H 2P 0 4+ K oH P 0 4, N a„S 0 4, N a c itra te , (N H 4)2S 0 4,M g S 0 4.
I N . F u rth e r so lu b ility m easu rem en ts a t 25° a re recorded. Haemoglobin behaves as a b iv a le n t acid or base on e ith e r side of th e p B of m in. so lu b ility (6-6).
A n e q u a tio n is deduced re la tin g th e to ta l solubility to
t h a t of th e n e u tra l m ol. in term s of th e a p p a re n t dissociation consts. T he la tte r a n d also th e iso electric p o in t v a ry w ith electro ly te concn. T he so lu b ility of caseinogen in NaCl-f- N aO H or HC1 also in d icates b ehaviour as a b iv a le n t acid or base.
A. Co h e n.
O xidation of haem oglobin b y m eth ylen e-b lu e.
O. Wa r b u r g a n d A. Re i d (Biochem . Z., 1931, 242, 149— 158).—T h e reversible re a c tio n betw een m e th y l
ene-blue (1 m ol.) a n d haemoglobin (2 m ol.) is followed m an om etrically, th e sub stan ces being m ix ed in a n a tm . of CO. W h en haemoglobin a n d CO are in equilibrium , v e ry little free haemoglobin exists. I f m ethylene-blue is th e n added, m ethsem oglobin is form ed, th e re a c tio n again com ing to a n equilibrium . If, how ever, th e free m etluem oglobin is rem oved from so lu tio n b y a d d itio n of H C N , th e process goes m uch fu rth e r. M + 2 H b C O + 2 H C N M H 2+ 2 H b C N + 2CO. O x idation of haemoglobin is th erefo re m easured b y elim ination of CO (positive pressure) an d red u ctio n of m ethaem oglobin b y ab so rp tio n of CO (negative p ressure). P . W . Cl u t t e r b u c k.
M ethaem oglobin and o x yg en . W . He u b n e r
(Biochem . Z., 1931, 241, 49 3 ; cf. M ichaelis, A ., 1931, 1319).— I n som e of th e experim ents of th e a u th o r a n d R h o d e (A., 1924, i, 229) lig h t a n d b a c te ria w ere n o t excluded a n d hence th e ex p lan atio n s of M ichaelis can b e applied. W . McCa r t n e y.
D eterm in atio n of p la sm a vo lu m e. I. D ye m eth od . S. Gr a f f a n d H . T . Cl a r k e. II. R ate of dye m ix in g . S. Gr a f f, D . A. D ’Es o p o, and A. J . B. Ti l l m a n (Arch. I n t. M ed., 1931, 48, [i], SOS—
820, 821— 827).:—I . T h e concn. of K 2C20 4 producing m in. cren atio n a n d haemolysis in blood is 1% . T he o p tic al ab so rp tio n of b rillian t-v ita l-red solutions is increased b y colloids a n d decreased b y electrolytes, th e region of m ax. a b so rp tio n being also changed.
T he spectropliotom etric e v alu atio n of th e d ye c o n te n t in p lasm a in presence of oxyhsem oglobin is described.
I I . Follow ing in tra v e n o u s in jectio n of th e dye, th e concn. a tta in s a m ax . a n d th e n falls to a n equilibrium v al. w ith in 6 m in. d ue to v a ry in g ra te s of circu latio n in different p a rts of th e system . T he concn. th e n decreases a t th e ra te of 10— 20% p e r h r. D ivergences m a y occur in p reg n an cy a n d p athological cases.
F . O. H o W IT T .
D eterm in ation of a lb u m in -g lo b u lin ra tio s in h u m an seru m . W . R . Ca m p b e l l a n d M. I . Ha n n a
(T rans. R o y . Soc. C anada, 1931, [iii], 25, V, 29— 31).—
T h e m eth o d depending on th e d ete rm in a tio n of to ta l seru m -p ro tein b y K je ld a h l d e term in atio n of N a n d of alb u m in in a sim ilar fashion a fte r rem oval of globulins b y N a 2S 0 4 is ap p lied to a ra p id m odification su itab le fo r clinical purposes. F . 0 . Ho w i t t.
C onversion of seru m -a lb u m in into ser u m - g lo b u lin . A. Fi s c h e r (N aturw iss., 1931, 19, 965—
966).:—P ro te in s form a com plex w ith h ep arin , th e com position of w h ich varies w ith th e concn. of h e p a r in ; th e so lu b ility of th e p ro te in s is th e re b y increased a n d th e isoelectric p o in t is sh ifted to th e acid side.
A d d itio n of h e p a rin to a solution of a lb u m in a t p a 5 gives a p p t. w hich h as all th e p ro p e rtie s of a euglob- ulin, pro v id ed t h a t th e p ro te in is in e x c e ss; f u r th e r
7 4 B R IT IS H C H EM ICA L A BSTRA C TS.— A .
a d d itio n of hep arin causes, th e globulin to dissolve.
T he fa cts su p p o rt Sorensen’s th e o ry of th e re v ersi
b ility of a dissociable p ro te in system .
P . G. Ma r s h a l l.
M ol. w ts . of the p rotein s in th eir native sta te.
T. Sv e d b e r g (N ature, 1931, 128, 999— 1000).— Re- d eterm in atio n s of sed im en tatio n consts. [by B.
SjOg r e n a n d Miss I. B. Er i k s s o n] show t h a t seru m - alb u m in and -globulin, am an d in , phycocyan, phyco- e ry th rin , a n d luem ocyanin possess th e sam e m ol. w ts.
w h eth er n ativ e or purified. I n o th e r cases, th e actio n of (N H.i)2S 0 4, used in th e p urification process, resu lts in aggregation. Haemoglobin is n o t affected by (N H 4)2S 0 4. L. S. Th e o b a l d.
D eterm in ation of oxid ised glutath ion e [in blood ]. R elation b etw een o xid ised and reduced glutath ion e. H . L. Ma s o n (Proc. Staff M eetings M ayo Clinic, 1931, 6, 16S— 169).— T h e H 2W 0 4 e x tra c t (25— 50 c.c.) is ev ap o rated u n d er reduced pressure to 1 c.c. or le s s ; th e residue is e x tra c te d w ith HOI in E tO H , an d th e E tO H e x tra c t (after c e n tri
fuging), o r an aliq u o t p o rtio n , is ad d ed to N a -H g and H g a t 0°, 51V-HC1 being add ed dropw ise. T he solution is d ilu ted , tre a te d w ith K I an d sta rc h , titr a te d w ith 0-01A -I to a blue colour, and titr a te d back to colourless w ith 0-002iV-Na2S203. A colori
m etric procedure is described. T he blood filtrates are p re p ared by a slight m odification of F olin and W u’s m ethod. T he am o u n t of oxidised g lu ta th io n e in o x ygenated blood is 20— 50% of th e to ta l.
Ch e m i c a l Ab s t r a c t s.
A n titryptic factor in h um an b lo od -seru m . W . Co r n e l i (Biochem. Z., 1 9 3 1 , 2 4 2 , 61—6 6 ).— T he hydrolysis of v ary in g am o u n ts of th e serum by v a ry in g a m o u n ts of purified try p sin is in v estig ated .
P . W . Cl u t t e r b u c k.
A ctivation of R o b iso n ’s h ex osem on op h o s- phoric acid in red cells and th e p reparation of activatin g en zym e solu tion s. O . Wa r b u r g and W . Ch r i s t i a n (Biochem . Z.. 1931, 2 4 2 , 206— 227).—
M ethternoglobin in red cells oxidises glucose, b u t m ixed w ith glucose in vitro does n o t re act. If red cells are haunolysed w ith H aO, th e stro m a ta rem oved b y centrifuging, an d glucose added to th e clear c e n tri
fugate, n e ith e r Oa u tilisatio n n o r glycolysis re su lts no r are th e cell reactio n s w ith m ethylene-blue an d m etluem oglobin o b tain ed . If , how ever, glucose is replaced b y R obison's hexosem onophosphoric acid, th e n th e clear ce n trifu g a te behaves to w ard s m ethylene- blue an d m ethternoglobin like th e in ta c t cell, th e resp iratio n being as g re a t o r g reater. I f th e c e n tri
fu g a te is tr e a te d w ith A l(OH)s a n d centrifuged, it is in a c tiv a te d in respect to hexosephosphate. A c tiv atio n requires th e presence of a t least tw o substances, th e isolation of d ry preps, of each of which is described, a n d in v irtu e of th e ir p ro p erties th e y are regarded as enzym e an d co-enzym e. I n enzym e—co-enzym e solutions, hexosem onophosphate is a tta c k e d n o t only b y m etluem oglobin a n d m ethylene-blue, b u t also by O j, ac tiv a tio n th e n carry in g th e reac tio n fu rth e r th a n it goes u n d e r physiological conditions. T his ov er
a c tiv a tio n explains w hy a n ox id atio n m a y lie sensitive to CO a n d HCN in th e cell, b u t m a y n o t b e so sensitive in th e enzym e solution. P . W . Cl c t t e r b c c k.
E ffect of so d iu m chloride on the activity of b lood -catalase in v iv o . G. M. Sa v o s t j a n o v (Bio
chem . Z., 1931, 241, 409— 412).—T h e ca talase co n te n t of th e blood of ra b b its is n o t ap p reciab ly affected by in trav en o u s a d m in istra tio n of 0-85% aq. N aCl or by oral a d m in istra tio n of 20% solution, a lth o u g h 10% solution caused rap id , an d th e 20% slow, increase in th e Cl c o n ten t. Since, in vitro, th e catalase c o n te n t is ap p reciab ly red u ced even b y 0-1% NaCl th e re m u st be p ro te c tiv e influence in th e blood in vivo.
W . McCa r t n e y.
C hem ical com p o sition of the b lood of C a m e lu s B a c tr ie n s . C. T. L oo (Chinese J . P hysiol., 1931, 5, 377— 380).—T he re su lts of th e d e term in atio n of th e various co n stitu e n ts of heparinised or ox alated cam el’s blood are recorded, an d com pared w ith vais, fo r horse, ox, sheep, a n d m an . N on-protein-N , urea-N , Cl', a n d inorg. a n d to ta l P are high, w hilst uric acid and
lipoid P are low. A. Co h e n.
B lo o d -su g a r . E . J . Bi g w o o d an d A. Wu i l l o t
(Com pt. rend. Soc. Biol., 1 9 3 0 ,1 0 4 , 329— 331 ; Ghem.
Z en tr., 1931, i, 3697).— H a g ed o rn ’s reag en t oxidises a su b stan ce, p ro b a b ly of th e g lu tath io n e series, w hich is n o t oxidised in F o n te s a n d T hivolle’s m ethod. T he su b stan ce is p re se n t only in th e ery th ro c y te s.
A. A. El d r i d g e. (a) S ta te of th e b lo o d -su g ar a s shown, by com p en sa tion d ia ly sis in v iv o , (b) N atu re of th e b lo o d -su g ar a s sh ow n b y a com p a riso n of th e o p tical rotation and th e red u cin g p ow er of the in v iv o d ia ly sate. M. H . Po w e r an d C. H . Gk e e n e (J. Biol. Chem., 1931, 94, 281—293, 295—
305).— (a) A m odified ty p e of th e a p p a ra tu s of A bel (A., 1914, i, 217) w as in serted betw een th e fem oral vein a n d a rte ry on each side of dogs, th e d ialy sa te liquids being w ith o u t glucose on one side (d ialy sate A ) an d containing 0-20% on th e o th e r (d ialy sate B ).
A fter 4 h r. vividiffusion th e glucose co n te n ts of A an d B a tta in e d a com m on level of 0-12— 0-13% , th e val. of th e plasm a-sugar. T he use of E t 20 fo r anæ sthesia p roduced irreg u lar re su lts owing to its effect on th e blood-sugar. T he reducing su b stan ces in th e dialvsates w ere alm o st to ta lly ferm entable.
H ence th e plasm a-glucose is freely diffusible (ef. A ..
1921, i, 2 8 6 ; 1922, i, 291, 2 9 5 ; 1931, 754). T he p lasm a-su g ar is alw ays h ig h er th a n th e corpuscular sugar, w hich is fairly const, ov er a considerable ran g e of concn. of plasm a-glucose. N o red istrib u tio n of glucose betw een th e cells an d plasm a occurs in blood on w ith d raw al.
(b) D ialysates .4 a n d B (see above) rem ained co n st, in ro ta to ry pow er fo r periods u p to 312 hr. T h e average vais, o b tain ed , expressed as glucose, w ere 0-01—
0-04% low er th a n th o se given by th e reducing pow er.
H ence sub stan ces undergoing spontaneous m u ta ro ta tio n w ere n o t p re sen t. A cidification to p H 2 of th e dialy sates produced a m ark ed an d im m ed iate increase in th e ro ta tio n w hich th e n agreed w ith th e vais, based on reducing pow er (cf. A ., 1926, S61). T h is change in ro ta tio n w as p a rtly reversible. H ence in blood only 33-glueose is p re se n t, o th e r substances such a s lactic acid playing a p a r t in th e o p tical phenom ena, especially a t c e rta in ranges of [H ‘j.
F . O. HO W I T T .
B IO C H E M IS T R Y . 7 5
D eterm in ation of true b lood -su g ar w ith o u t y ea st. A. Fu j i t a an d D. Iw a t a k e (Biochem . Z., 1931, 242, 43 —60).— A new deproteinising m eth o d by m eans of Cd(OH)2 gives filtra tes which, since th e y are free from g lu tath io n e, ergothioneine, a n d uric acid, give tru e blood-sugar vals, by a n y of th e usual m ethods. A n iodom etric d eterm in atio n using K 3Fe(C N )6 is described. The reducing pow er of glu tath io n e varies w ith its concn. an d th e presence or absence of sugar. I n presence of considerable am o u n ts of g lu ta th io n e , th e y e a st m eth o d does n o t give correct sugar vals. T he H a g e d o rn -Je n se n m e th o d alw ays gives to o high resu lts. P . W . Cl u t t e r b u c k.
C om bined su g a r of tu n g stic acid filtra tes of blood. F . H . Sc h a r l e s a n d E . S. We s t (J. Biol.
Chem., 1931, 93, 359— 364).—T he presence of a hydrolysable sugar com plex in tu n g stic acid filtrate s of blood (T om psett, A ., 1930, 1306) is n o t confirm ed.
On acid hydrolysis of such filtrates, th e ferm entable sugar rem ains unchanged, w h ilst th e non-ferm entable reducing substances increase to a m ax. in 5 hr. and finally fall below th e original val. in 20 hr. T h is is n o t due to g lu tath io n e, b u t to u n stab le reducing m a terial form ed du rin g hydrolysis. Since p p tn . by H g S 0 4- B a C 0 3 com pletely rem oves th e non- ferm en tab le reducing su b stan ce a t a n y p o in t in th e hydrolysis, th e re is no sugar in a n y form in tu n g stic
acid filtrates. A. Co h e n.
P icr ic acid b lo o d -su gar m eth od after zin c p recip itation . V. C. My e r s a n d C. W . R . Ro o t
(J. L ab. Clin. Med., 1931,16, 890—897).—T he filtra te a fte r p p tn . of blood-proteins w ith Z n S 0 4 a n d N aO H is s a tu ra te d w ith picric acid a n d analysed b y M yers an d B ailey’s m eth o d (A., 1916, i, 300). N o n glucose reducing su bstances are p p td . b y th e Z n S 0 4.
Ch e m i c a l Ab s t r a c t s.
D eterm in a tion of free, p rotein -, and com bin ed n on -p rotein -su gar in n o rm a l and p ath olo gical ser u m , urine, and b ody-fluid s. B. Lu s t i g an d A.
La n g e r (Biochem. Z., 1931, 242, 320— 337).— B y m odifications of th e m eth o d of T illm ans a n d P h ilip p i (A., 1930, 108) th e v ario u s sugar fractio n s can be determ in ed in sm all a m o u n ts (0-05— 0-4 c.c.) of th e fluids m entioned. H ydrolysis is u n necessary a n d th e errors of o th e r m eth o d s are avoided. The procedure has been applied to d e term in atio n s in th e fluids from persons suffering from various diseases.
W . McCa r t n e y.
A lteratio n s in th e rotation and m u tarotation of glu co se. II. E ffect of s a lts and organ ic su b sta n ces. H . N . Na u m a n n (Biochem. Z., 1931, 242, 259—265; cf. A .,1931,1275).—U n d er usual experim en
ta l conditions th e sa lts used for d eproteinisation, p re vention of coagulation of blood, a n d clarification have no effect on th e ro ta tio n of glucose solutions. The ro ta tio n is affected b y E tO H a n d AcOH, b u t n o t by su bstances u su ally p re se n t in body-fluids (urea, creatine, creatinine, uric acid). W . McCa r t n e y.
G asom etric d eterm in ation of la ctic acid in the b lo o d . B. F . Av e r y a n d A. B. Ha s t i n g s (J. Biol.
Chem., 1931, 94, 273— 280).—B lood or serum (1 c.c.) is d ep ro tein ised b y H 2W 0 4, th e filtra te freed from ca rb o h y d ra tes b y tre a tm e n t w ith C u S 0 4 a n d Ca(OH)2 (A., 1918, ii, 86), a n d th e lactic acid in th e so lu tio n
d eterm in ed b y o x id atio n to C 0 2 b y K M n 0 4, using th e m an o m etrie gas a p p a ra tu s of Van Siyke (A., 1927, 800). A correction for C 0 2 evolved from some u n know n su b stan ce is applied. F . 0 . Ho w i t t.
Influence of fat d ep rivation and feed in g on th e d istrib u tion of b lo od -lip in s. S. M. Li n g
(Chinese J . P hysiol., 1931, 5, 381— 397).—T he lip in co n te n ts of whole blood a n d p lasm a hav e been d e te r
m ined for tw o dogs on d iets v a ried in f a t co n ten t.
Corpuscle vals. were determ ined in directly. R em oval of f a t from a m ixed d ie t causes a decrease in blood- lipins o th e r th a n lecithin a n d cholesterol. D u rin g fastin g a bigger red u ctio n in blood-fat occurs, in which lecithin a n d cholesterol are m ain ly affected. 6— 7 hr.
a fte r ingestion of olive oil all lipoid c o n stitu e n ts are increased, to a g re a te r e x te n t, generally, in th e plasm a.
I n th e tra n s p o rt of absorbed fa t, lecith in an d chole
stero l ap p e a r to be em ployed. A. Co h e n.
D eterm in ation of ch olestero l in w h o le b lood.
J . C. Fo r b e s a n d H . Ir v i n g (J. L ab. Clin. M ed., 1931.
16, 909— 912).— A m odification of th e m eth o d em ployed for p lasm a an d serum (A., 1931, 1080).
Ch e m i c a l Ab s t r a c t s.
M icro-d eterm in ation of lecith in in b lood and p la sm a . W . Li n t z e l an d G. Mo n a s t e r i o (Bio
chem . Z., 1931, 241, 273—279; cf. A ., 1931, 1178).—
T he m eth o d p reviously described has been m odified a n d applied to th e d e te rm in atio n of lecithin in 10 c.c.
of blood or plasm a. T he NMes lib e rate d from choline derived from th e lecithin is determ in ed by titra tio n . R e su lts fo r horse, sheep, an d h u m a n blood a n d p lasm a show t h a t th e lecith in c o n te n t of th e p lasm a is slig h tly low er th a n th a t of th e whole blood.
W . McCa r t n e y.
S en sitiv ity of m eth o d s for d eterm in ation of ch olesterol, p h osp h oru s, and calciu m in the sa m e sa m p le of b lo od -seru m . G. H . Ba r i l and J . La b a r r e (T rans. R oy. Soc. C anada, 1931, [iii], 25, V, 43— 44).—T he m eth o d of th e a u th o rs for th e d e te rm in a tio n of Ca (A., 1931, 377) is applicable to a concn. of n o t less th a n 0-005% , th e sta n d a rd colori
m etric m e th o d for cholesterol to one of n o t less th a n 0-004% , a n d th e m eth o d of B enedict a n d Theis (A., 1924, ii, 700) for P to n o t less th a n 0-5 c.c. of serum .
F . 0 . Ho w i t t.
N o r m a l v aria tio n s in the in org an ic p hosp h oru s of th e b lood of dairy cattle. L. S. Pa l m e r, W . S.
Cu n n i n g h a m, a n d C. H . Ec k l e s (J. D airy Sci., 1930, 1 3 ,174— 195).— D aily, a n d p ro b ab ly h o urly, v ariatio n s occur in th e inorg. P co n ten t of th e blood of d a iry c a ttle . V als. are affected slig h tly b y feeding, b u t n o t appreciably b y drinking. E xercise produces a slight increase in b lo o d -P 0 4" ', followed b y a m ark ed decline lastin g for several hr. P a rtu ritio n causes a consider
able decline in b lo o d -P 0 4" '. Calf blood, a t b irth , shows higher vals. th a n t h a t of th e dam , a n d la te r increases w ith age u p to 6 m o n th s, su b seq u en tly declining ste a d ily to th e n o rm al val. of a d u lts.
A. G. Po l l a r d.
N o r m a l v ariatio n s in th e calciu m con tent of th e b lood of dairy cattle. L . S. Pa l m e r an d E . C.
Ec k l e s (J. D airy Sci., 1930, 13, 351— 359).— D aily v a ria tio n s occur in th e Ca c o n te n t of th e blood- pla sm a of d a iry c a ttle , a lth o u g h a high coeff. of
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B R IT IS H CH EM ICA L A BSTRA C TS.— A .co rrelatio n ex ists in vals. on successive days. I n sam ples ta k e n on 3 successive days d ev iatio n s in Ca co n te n ts from th e th eo retica l are n egative w hen th e plasm a-C a is low a n d positive w hen i t is high.
A. G . Po l l a r d.
B io m etr y of calciu m and in organ ic p hosp h oru s in the b lood -p lasm a of d airy cattle. L. S.
Pa l m e r, R . A. Go r t n e r, an d R . Ru d e (J . D a iry Sci., 19 3 1 ,1 3 , 360— 367).— T here is no correlation betw een th e Ca a n d inorg. P co n te n ts of th e blood-plasm a of d a iry c a ttle , an d no significant am o u n t of Ca p h o sp h ate
Pa l m e r, R . A. Go r t n e r, an d R . Ru d e (J . D a iry Sci., 19 3 1 ,1 3 , 360— 367).— T here is no correlation betw een th e Ca a n d inorg. P co n te n ts of th e blood-plasm a of d a iry c a ttle , an d no significant am o u n t of Ca p h o sp h ate