The distribution of avidin

The distribution of avidin

Life Sciences ~Qo. 11, pp . 621-623, 1962 " United States .- Pergemon Press, Inc. Printed in the THE DISTRIBUTION OF AVIDIN Peter D . Jones and Mic...

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Life Sciences ~Qo. 11, pp . 621-623, 1962 " United States .-

Pergemon Press, Inc.

Printed in the

THE DISTRIBUTION OF AVIDIN Peter D . Jones and Michael H. Briggs*' Victoria University of Wellington New Zealand (Received 8 October 1960 AVIDIN is s protein first detected in the white of hen's

egg .l

It has been

crystallized from this source and shown to be a basic protein of molecular weight ca . 66,000 .2

Avidin forms a stable complex with biotin :

the interaction

occurring both in vitro and in vivo on the feeding of raw egg white to an animal .3 For this reason the raw white of hen's egg is toxic to a wide range. of animals .



Previous workers$' 9 have shown that avidin-like proteins occur in the egg whites of several other avian species .

D.ius Hertz and Sebrella reported the

following avidin concentrations for dried egg whites : duck 7.1, goose 8.0 .

hen 11 .5, turkey 16 .2,

~ese results are expressed in avidin units per gram .

A

unit of avidin activity is defined as that amount of avidin that will combine with one microgram of pure d-biotin . ~eae findings indicate that avidin-like proteins :my be a common constituent of bird egg-whites .

We have consequently examined for avidin, specimens of egg

whites from species representing e11 the major avian families . 7~e assay method used Lactobacillus arabinosus 17-5, obtained Pram the American ~rpe Culture Collection, as test organism . lO medium for biotin assay.

It was graven on "Difco"

Avidin activity was determined by measuring bacterial

growth in tubes containing 1.0 ml of egg white and varying amounts of d-biotin . Results of these experiments are given in Table 1 .

It is apparent that

avidin proteins are present in all ; with the possible exception of the herring

Present address :

Jet Propulsion Laboratory, California Institute of Zlechnology, Pasadena, California, U.S .A . 621

~ DIS~IBtfrION OF AV.mIId

622

No .ll

TART.R 1

Avidin Content of Egg Whites

Bird

Family

Avidin content (units per gram dried weight)

1

English Sparrov

Passer dameaticus

Ploicidae

7.2

2

Ostrich

Struthio csmchis

Struthidae

1.7

3

Herring Gull

Larus argentatus

Iari dae

0.1

4

Great Gbrmorant

Phalacrocorax carbosinensis

Phalacrocoracidae

2.6

5

Grackle

~Ziscalus quiscula

Icteridae

8.3

6

Adelie Penguin

Pygoacclis adelige

Spheniscidae

5 .0

7

Robin

làrdus migratorius

Turdidae

3 .8

8

European Coot

Fulica atra

Rallidae

~+ .3

9

Crow

Corvus brachyrhynchos

Corvidae

7.5

10

Altami Heron

Altamis altarm

Ardea

2 .8

11

Red-throated Loon

Gavia stellata

Gavüdae

2 .0

12

Starling

3turnus vulgaris

Sturnidae

6 .1

13

Zebra Finch

Z1a.eaiopygia castanea

Ploccidae

7.~+

14

Budgerigax

Melopsittacus undulatus Psittacidae

During a search for avidin-like proteins, Woolley and Longsworth

6 .8 11

reported

that protamiae, a crystalline po].ypeptide of salmon sperm, possessed weak avidin activity :

approximately 0.1 - 0.2 per cent of the activity of pure avidin oa a

dry weight basis .

We have confirmed this finding and have also assayed fresh

bull sperm for biotin-binding capacity.

We find that this material possesses

0.02 units of avidin activity per gram fresh weight .

We were unable to detect

avidia activity is dried sperm. Zhe discovery of biotin-binding proteins in egg whites and in sperm Pram quite different groups of saimals suggests that gvidia proteins may be very

THE DISTRIBUTIOA OF AVIDIN

No . 11

623

irl.dely distributed in the animal kingdom, and moreover may play some fundamental role in the physiology of reproduction . Acknowle nt - We are most grateful to Professor C. G. Sibley of Cornell University for t e generous gift of egg ~rhite samples . References 1.

R. E. EAKIN, E . E. SftELL and R. J. WILLIAMS, J. Biol . ~em. 136, 201 (1940) ; 535 (1941) .

2.

H. ERAII~TI~-CONRAT et al ., Arch . Biochem. Biophys . ~, 80 (1952) .

3.

M. A. BOAS, Biochem. J. 21, 712 (l927) .

4.

S. G . SMI'~, Science 100, 389 (194~+)"

g.

H. RAUCH and W. B. RUtTIIiG, Experientia 14, 3~ (1958) "

6.

P. S. SARMA, Indian J. Med. Res. ~, 149 (1944) .

7.

W. P . LEHRER, A. C.

8.

R . HERTZ and W. H. SERRELL, Science ~6, 257 (1942),

9.

R . E. FEQ~7C et al ., J. Biol . Gliem. 2~, 2307 (1960) .

10 .

L. D. WRIGHT and H. R. SKEGGS, Proc . Soc. Exp. Biol . Med. ~, 92 (l944) .

11 .

D. W. WOOLLEY e~nd L. G. IAHGSWOiRTH, J. Biol . (~em . 142, 285 (1942) .

WTF'4F

and P. R . A9DORE, J. ftutr . 47, 203 (1952) .