originalFil: Dallner, Gustav. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Behrens, Nicolás H.. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Parodi, Armando José A.. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaFil: Leloir, Luis Federico. Instituto de Investigaciones Bioquímicas Fundación Campomar; ArgentinaBlanco y negro3 páginas en pdfLFL-PI-O-ART. Artículos científicosUnidad documental simpleAR-HYL-201

Armando J. Parodi

Behrens

Bergstrand

Burgos

Coleman

Dallner

Glaumann

Gustav Dallner

Lowry

Luis F. Leloir

Morré

Nicolas H. Behrens

Richards

Sottocasa

Widnell

FEBS Letters

English

Fil:Behrens, N.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Parodi, A.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina

Dallner, G.

Behrens, N.H.

Parodi, A.J.

Leloir, L.F.

Rectorado de la Universidad de Buenos Aires

Subcellular distribution of dolichol phosphate

Dallner, Gustav

Behrens, Nicolás H.

Parodi, Armando José A.

Leloir, Luis Federico

LAReferencia - Red Federada de Repositorios Institucionales de Publicaciones Científicas Latinoamericanas

Volume 24, number 3 FEBSLETTERS August 1972 SUBCELLULAR DISTRIBUTION OF DOLICHOL PHOSPHATE Gustav DALLNER*, Nicolas H. BEHRENS, Armando J. PARODI and Luis F. LELOIR Institute de Investigaciones Bioquimicas “Fundacibn Campomar” and Facultad de Ciencias Exactas y Natwales, Obligado 2490, Buenos Aires (28), Argentina Received 12 June 1972 1. Introduction A crude preparation of liver microsomes was shown to catalyze the transfer of glucose from UDP-Glc to Dol-P** to form Dol-P-Glc [ 1 ] . ~ub~quently it was observed that microsomes also transferred the glucose from Dol-P-Glc to an endogenous acceptor. This latter compound is probably another dolichol derivative containing about 20 monosaccharide units bound to dolichol through a phosphate or pyrophosphate bridge [2,3]. The abbreviation Glc-acceptor will be used for this dolichol derivative until the details of its structure are known with certainty, Liver microsomes also catalyze the transfer of mannose to Dol-P from GDP-mannose and of N-acetyl ~ucos~ine from UDP-GlcNAc to form what seems to be dolichol monophosphate mannose and dolichol monophosphate N-aeetyl glucosamine [4, S] . It is possible that the dolichol derivatives are inter- mediates involved in the synthesis of the sugar portions of the various glycoproteins and glycolipids occurring in smooth microsomes, the Golgi system and other cellular membranes. It is therefore necessary to establish the subcellular loc~ization of these derivatives. * Permanent address: Department of Pathology II, Karolinska institutet, Stockholm, Sweden. ** Abbreviations., Dol-P, dolichol monophosphate. Dol-P-Glc, dolichol monophosphate glucose. G&acceptor, the glucosylated form of an endogenous acceptor. North-Holland Publishing Company - Amsterdam The present work reports the subcellular distribu- tion of Dol-P and of two enzymes related to its utilization, 2. Materials and methods Radioactive UDP-Glc and Dol-P-Glc were prepared as earlier described [ 11. Dol-P from whole liver and from the subcellular fractions was extracted and purified up to the DEAE-cellulose step as previously described [ 1 ] . The conditions for enzymatic assays are given in the text of each table. The preparation of subcellular fractions from rat liver was done according to the following procedures described earher: ,luclear fraction [6], plasma mem- branes [7], Golgi system [8,9], total as well as inner and outer mitochondrial membranes [lo] , and total microsomes and microsomal subfractions [ 11, 121. Protein [ 131 and phospholipid [ 141 were deter- mined as aSready described. 3. Results and discussion The Dol-P content of the isolated subcellular fractions was determined enzymatically. It had been found that the amount of Dol-P-Glc formed in the reaction UDP-Glc + Dol-P -+ Dol-P-Glc + UDP is pro- portional to the concentration of Dol-P present [I 1. Using labelled UDP-Glc very small amounts of Dol-P 31s Volume 24, number 3 FEBS LETTERS August 1912 Table 1 Dol-P content of subcellular fractions isolated from rat liver. Dol-P (in units per mg of phospholipid) Nuclear 55.5 Plasma membranes 9.9 Golgi 42.1 Total mitochondria 12.3 Inner membranes 11.8 Outer membranes 10.6 Total microsomes 21.1 Rough 38.1 Smooth I 20.2 Smooth II 25.1 The Dol-P elicited increase in formation of Dol-P-Glc was measured with an incubation mixture which contained: 0.15 M Trismalate, pH 1.7, 0.8% Triton X-100, 6 mM Mg-EDTA, 6 mM MgCla, 0.12 M 2-mercaptoethanol, 15 ~1 of a total microsomal fraction (0.5 mg protein), [14C] UDPG (150,000 cpm, 309 Ci/mole) and increasing amounts of Dol-P, isolated from the subcellular fractions in a final volume of 165 ~1. After 15 min incubation at 37”, the mixture was processed as previously described 131. The increase of lower phase soluble radioactivity above endogenous activity by Dol-P isolated from 70 mg wet weight of whole liver homo- genate, is defined as 10 arbitrary units. The endogenous activity obtained in the absence of externally added Dol-P was subtracted. can be detected so that this reaction was used as an assay for Dol-P [3]. Results obtained show that Dol-P or a substance that mimics its action is found in all subcellular frac- tions with its highest concentration in nuclei, the Golgi fraction and rough microsomes and lowest in mitochondria and the plasma membrane (table 1). Morton et al, [ 1.51 studied the subcellular distribution of non-phosphorylated dolichol occurring as the free alcohol or esterified with fatty acids in pig liver. Expressed on a protein basis they also found a higher concentration of dolichol in the nuclear fraction than in either the mitochondrial or microsomal fractions. Activities of the enzymes involved in the reaction sequence: UDP-Glc -l-+ Dol-P-Glc -2, (X-acceptor, were measured. Table 2 shows data in which steps 1 and 2 were measured simultaneously, that is, using UDP-Glc as substrate, and also data in which direct transfer from Dol-P-Glc was assayed. The measure- ment of enzyme activity catalyzing the second step is based on the assumption that the acceptor for the glucose from Dol-P-Glc occurs in excess in each sub- fraction. However, this assumption cannot be verified until a method is found for separately assaying the acceptor. The highest specific activity for transfer from UDP-Glc to Dol-P (step 1) is present in the outer mitochondrial membranes and smooth I microsomes while in the nuclear and Golgi fractions as well as in the rough and smooth II microsomes the activity is one half of the former. The transferase seems to be absent from plasma and inner mitochondria mem- branes. However negative results may reflect enzyme inactivation caused during the rather involved isolation of the membranes. The distribution of the activity catalyzing step 2 depends on the way the reaction is measured. When starting from UDP-Glc the Golgi system and the smooth microsomes were the most active fractions. The nucleus also showed some activity. Vihen meas- uring the direct transfer from Dol-P-Glc, a somewhat different distribution was found. Significant activity is detected only in the microsomes with some activity also in the plasma membranes. The remaining fractions gave only marginal activities. Parallel measurements of water soluble radioactivity in the Folch upper phase (see table 2), excluded the possibility that the absence of activity in some fractions could be due to a breakdown of the Glc-acceptor as observed previous- ly [S] . The differences, depending on how step 2 was measured, were not unexpected since assay conditions were not the same. However, the data are consistant in showing that mitochondria possess no transferase for step 2 and that some activity does exist in plasma membranes. Summing up, it has been found that Dol-P and enzymes catalyzing the formation of Dol-P-Glc and the subsequent glucosylation of another dolichol intermediate, are widely but unevenly distributed in liver subcellular membranes: At this stage we can only venture to say that Dol-P plays different roles in the different liver membranes. 3 I 6 Volume 24, number 3 FEBS LETTERS August 1972 Table 2 Transfer of glucose from UDP-Glc and from Dol-P-Glc. Substrate UDP-Glc Dol-P-Glc Product Dal-P-GIc Glc-acceptor Glc-acceptor Water soluble (pmoles of glucose transferred per mg of protein) Nuclear fraction 6.9 0.4 0 0 Plasma membranes 0.3 0.05 0.6 0 Golgi fraction 5.2 1.6 0.2 0 Total mitochondria 2.1 0.1 0.01 0 Inner membranes 0.6 0.03 0 0 Outer membranes 16.9 0.15 0.02 0 Total microsomes 9.4 0.9 3.3 1.0 Rough microsomes 8.3 0.9 1.6 0.8 Smooth 1 microsomes 17.6 1.1 1.3 0.3 Smooth II microsomes 9.3 OS 0.1 0.1 For the measurement of Dol-P-Glc and Glc-acceptor formation from UDP-Glc, the incubation mixture contained: 0.33 M Tris- maleate pH 7.7,0.6% Triton X-100, 30 mM Mg-EDTA, 30 mM MgCls, 0.1 M mercaptoethanol, 10 ~1 of the appropriate subfrac- tion (0.5 mg of protein), [14C] UDP-Glc (75 000 cpm, 309 @‘mole) and iO0 units (see table 1) of Dal-P from total liver, in a final volume of 31 ~1. Incubations were performed at 37” for 20 min and then 0.4 ml of methanol, 0.6 ml of chloroform and 0.2 ml of 4 mM MgCla were added. After centr~ugation the upper phase was removed and the phase decanted. If done carefully the precipitate from the interphase remains in the tube. Both the interphase and the lower phase were washed twice with 4 mM MgCl2 in chloroform- methanol--water 3:48:47. The interphase was extracted three times with 0.5 ml of chloroform-methanol-water 1:1:0.3 121. This extract and the lower phase were transferred to aluminium planchets and counted in a gas flow counter. The reaction mixture for the direct transfer of glucose from Dol-PGlc to the acceptor containined: 70 mM Tris-maleate, pH 7.7, 0.18% deoxycholate, 3.5 mM Na-EDTA, 14 mM mercaptoethanol, [ 14C] Dol-P-Glc (2,000 cpm) and an aliquot of the isolated fractions containing 0.5 mg of protein, in a final volume of 140 ~1. After incubating for 15 min at 30”, 0.4 ml of methanol, 0.6 ml of chloroform and 0.2 ml of 4 mM MgCla were added. After centrifugation both the upper and lower phases were discarded and the remaining precipitate was washed again with the same methanol-chloroform-MgCla mixture. The Glc- acceptor was then extracted with three 0.5 ml portions of chloroform-methanol-water 1: 1:0.3. The extracts were counted as outlined above, In both assays appropriate blanks were made and subtracted. Acknowledgements This work was supported by grants from the Consejo National de Investigaciones CientiEcas y TBcnicas (Argentina). NHB and AJP are career in- vestigators of this latter institution. References [l] NH. Behrens and L.F. Leloir, Proc. Natl. Acad. Sci. U.S. 66 (1970) 15 3. [2] N.H. Behrens, A.J. Parodi and L.F. Leloir, Proc. Natl. Acad. Sci. U.S. 68 (1971) 1758. f 31 A.J. Parodi, N.H. Behrens, L.F. Leloir and M.A. Danker& Biochim. Biophys. Acta, in press. [4] J.B. Richards, P.J. Evansand F.W. Hemming, Biochem. J. 124 (1971) 957. [S ] N.H. Behrens, A.J. Parodi, L.F. Leloir and C.R. Krisman Arch. Biochem. Biophys. 143 (1971) 375. [6] CC. Widnelland J.R. Tata, Biochem. J. 92 (1964) 313. [7] R. Coleman, R.M. Mitchell, J.B. Fineau and J.N. Hawthorne, Biochim. Biophys. Acta 135 (1967) 573. [S] D.J. MorrB, R.L. Hamilton, H.H. Mollenhauer, R.W. Mahley, W.P. Cunningham, R.D. Cheetman and V.S. LeQuire, J. Cell BioI. 44 (1970) 484. ]9] H. Glaumann and J.L.E. Ericsson, J. Cell Biol. 47 (1970) 555. [lo] G.L. Sottocasa, B. Kuylenstierna, L. Ernster and A. Bergstrand, J. Cell Biol. 32 (1967) 415. [l l] G. Dallner, Acta Pathol. Microbial. Stand., Suppl. (1963) 166. f12] A. Bergstrand and C. Dallner, Anal. Biochem. 29 (1969) 351. 1131 O.H. Lowry, N.V. Rosebrough, A.L. Farr and R.J. Randall, BioL Chem. 193 (1951) 265. [ 141 G. Dallner, P. Siekevitz and G.E. Palade, J. Cell Biol. 30 (1966) 173. [15] J. Burgosand R.A. Morton, Biochem. J. 82 (1962) 454. 317 

CONICET Digital

Behrens, Nicolas H.

Parodi, Armando J.

Leloir, Luis F.

Elsevier - Publisher Connector 

Volume 24, number 3 FEBSLETTERS August 1972 
SUBCELLULAR DISTRIBUTION OF DOLICHOL PHOSPHATE 
Gustav DALLNER*, Nicolas H. BEHRENS, Armando J. PARODI 
and Luis F. LELOIR 
Institute de Investigaciones Bioquimicas “Fundacibn Campomar” 
and 
Facultad de Ciencias Exactas y Natwales, Obligado 2490, Buenos Aires (28), Argentina 
Received 12 June 1972 
1. Introduction 
A crude preparation of liver microsomes was shown 
to catalyze the transfer of glucose from UDP-Glc to 
Dol-P** to form Dol-P-Glc [ 1 ] . ~ub~quently it was 
observed that microsomes also transferred the glucose 
from Dol-P-Glc to an endogenous acceptor. This latter 
compound is probably another dolichol derivative 
containing about 20 monosaccharide units bound to 
dolichol through a phosphate or pyrophosphate 
bridge [2,3]. The abbreviation Glc-acceptor will be 
used for this dolichol derivative until the details of 
its structure are known with certainty, 
Liver microsomes also catalyze the transfer of 
mannose to Dol-P from GDP-mannose and of N-acetyl 
~ucos~ine from UDP-GlcNAc to form what seems 
to be dolichol monophosphate mannose and dolichol 
monophosphate N-aeetyl glucosamine [4, S] . 
It is possible that the dolichol derivatives are inter- 
mediates involved in the synthesis of the sugar portions 
of the various glycoproteins and glycolipids occurring 
in smooth microsomes, the Golgi system and other 
cellular membranes. It is therefore necessary to 
establish the subcellular loc~ization of these derivatives. 
* Permanent address: Department of Pathology II, Karolinska 
institutet, Stockholm, Sweden. 
** Abbreviations., 
Dol-P, dolichol monophosphate. Dol-P-Glc, dolichol 
monophosphate glucose. G&acceptor, the glucosylated 
form of an endogenous acceptor. 
North-Holland Publishing Company - Amsterdam 
The present work reports the subcellular distribu- 
tion of Dol-P and of two enzymes related to its 
utilization, 
2. Materials and methods 
Radioactive UDP-Glc and Dol-P-Glc were prepared 
as earlier described [ 11. Dol-P from whole liver and 
from the subcellular fractions was extracted and 
purified up to the DEAE-cellulose step as previously 
described [ 1 ] . The conditions for enzymatic assays 
are given in the text of each table. 
The preparation of subcellular fractions from rat 
liver was done according to the following procedures 
described earher: ,luclear fraction [6], plasma mem- 
branes [7], Golgi system [8,9], total as well as inner 
and outer mitochondrial membranes [lo] , and total 
microsomes and microsomal subfractions [ 11, 121. 
Protein [ 131 and phospholipid [ 141 were deter- 
mined as aSready described. 
3. Results and discussion 
The Dol-P content of the isolated subcellular 
fractions was determined enzymatically. It had been 
found that the amount of Dol-P-Glc formed in the 
reaction UDP-Glc + Dol-P -+ Dol-P-Glc + UDP is pro- 
portional to the concentration of Dol-P present [I 1. 
Using labelled UDP-Glc very small amounts of Dol-P 
31s 
Volume 24, number 3 FEBS LETTERS August 1912 
Table 1 
Dol-P content of subcellular fractions isolated from rat liver. 
Dol-P 
(in units per mg of phospholipid) 
Nuclear 55.5 
Plasma membranes 9.9 
Golgi 42.1 
Total mitochondria 12.3 
Inner membranes 11.8 
Outer membranes 10.6 
Total microsomes 21.1 
Rough 38.1 
Smooth I 20.2 
Smooth II 25.1 
The Dol-P elicited increase in formation of Dol-P-Glc was 
measured with an incubation mixture which contained: 
0.15 M Trismalate, pH 1.7, 0.8% Triton X-100, 6 mM 
Mg-EDTA, 6 mM MgCla, 0.12 M 2-mercaptoethanol, 15 ~1 
of a total microsomal fraction (0.5 mg protein), [14C] UDPG 
(150,000 cpm, 309 Ci/mole) and increasing amounts of Dol-P, 
isolated from the subcellular fractions in a final volume of 
165 ~1. After 15 min incubation at 37”, the mixture was 
processed as previously described 131. The increase of lower 
phase soluble radioactivity above endogenous activity by 
Dol-P isolated from 70 mg wet weight of whole liver homo- 
genate, is defined as 10 arbitrary units. The endogenous 
activity obtained in the absence of externally added Dol-P 
was subtracted. 
can be detected so that this reaction was used as an 
assay for Dol-P [3]. 
Results obtained show that Dol-P or a substance 
that mimics its action is found in all subcellular frac- 
tions with its highest concentration in nuclei, the 
Golgi fraction and rough microsomes and lowest in 
mitochondria and the plasma membrane (table 1). 
Morton et al, [ 1.51 studied the subcellular distribution 
of non-phosphorylated dolichol occurring as the free 
alcohol or esterified with fatty acids in pig liver. 
Expressed on a protein basis they also found a higher 
concentration of dolichol in the nuclear fraction than 
in either the mitochondrial or microsomal fractions. 
Activities of the enzymes involved in the reaction 
sequence: UDP-Glc -l-+ Dol-P-Glc -2, (X-acceptor, 
were measured. Table 2 shows data in which steps 1 
and 2 were measured simultaneously, that is, using 
UDP-Glc as substrate, and also data in which direct 
transfer from Dol-P-Glc was assayed. The measure- 
ment of enzyme activity catalyzing the second step is 
based on the assumption that the acceptor for the 
glucose from Dol-P-Glc occurs in excess in each sub- 
fraction. However, this assumption cannot be verified 
until a method is found for separately assaying the 
acceptor. 
The highest specific activity for transfer from 
UDP-Glc to Dol-P (step 1) is present in the outer 
mitochondrial membranes and smooth I microsomes 
while in the nuclear and Golgi fractions as well as in 
the rough and smooth II microsomes the activity is 
one half of the former. The transferase seems to be 
absent from plasma and inner mitochondria mem- 
branes. However negative results may reflect enzyme 
inactivation caused during the rather involved isolation 
of the membranes. 
The distribution of the activity catalyzing step 2 
depends on the way the reaction is measured. When 
starting from UDP-Glc the Golgi system and the 
smooth microsomes were the most active fractions. 
The nucleus also showed some activity. Vihen meas- 
uring the direct transfer from Dol-P-Glc, a somewhat 
different distribution was found. Significant activity 
is detected only in the microsomes with some activity 
also in the plasma membranes. The remaining fractions 
gave only marginal activities. Parallel measurements of 
water soluble radioactivity in the Folch upper phase 
(see table 2), excluded the possibility that the 
absence of activity in some fractions could be due to 
a breakdown of the Glc-acceptor as observed previous- 
ly [S] . The differences, depending on how step 2 was 
measured, were not unexpected since assay conditions 
were not the same. 
However, the data are consistant in showing that 
mitochondria possess no transferase for step 2 and 
that some activity does exist in plasma membranes. 
Summing up, it has been found that Dol-P and 
enzymes catalyzing the formation of Dol-P-Glc and 
the subsequent glucosylation of another dolichol 
intermediate, are widely but unevenly distributed in 
liver subcellular membranes: At this stage we can 
only venture to say that Dol-P plays different roles in 
the different liver membranes. 
3 I 6 
Volume 24, number 3 FEBS LETTERS August 1972 
Table 2 
Transfer of glucose from UDP-Glc and from Dol-P-Glc. 
Substrate UDP-Glc Dol-P-Glc 
Product 
Dal-P-GIc Glc-acceptor Glc-acceptor Water soluble 
(pmoles of glucose transferred per mg of protein) 
Nuclear fraction 6.9 0.4 0 0 
Plasma membranes 0.3 0.05 0.6 0 
Golgi fraction 5.2 1.6 0.2 0 
Total mitochondria 2.1 0.1 0.01 0 
Inner membranes 0.6 0.03 0 0 
Outer membranes 16.9 0.15 0.02 0 
Total microsomes 9.4 0.9 3.3 1.0 
Rough microsomes 8.3 0.9 1.6 0.8 
Smooth 1 microsomes 17.6 1.1 1.3 0.3 
Smooth II microsomes 9.3 OS 0.1 0.1 
For the measurement of Dol-P-Glc and Glc-acceptor formation from UDP-Glc, the incubation mixture contained: 0.33 M Tris- 
maleate pH 7.7,0.6% Triton X-100, 30 mM Mg-EDTA, 30 mM MgCls, 0.1 M mercaptoethanol, 10 ~1 of the appropriate subfrac- 
tion (0.5 mg of protein), [14C] UDP-Glc (75 000 cpm, 309 @‘mole) and iO0 units (see table 1) of Dal-P from total liver, in a 
final volume of 31 ~1. 
Incubations were performed at 37” for 20 min and then 0.4 ml of methanol, 0.6 ml of chloroform and 0.2 ml of 4 mM MgCla 
were added. After centr~ugation the upper phase was removed and the phase decanted. If done carefully the precipitate from the 
interphase remains in the tube. Both the interphase and the lower phase were washed twice with 4 mM MgCl2 in chloroform- 
methanol--water 3:48:47. The interphase was extracted three times with 0.5 ml of chloroform-methanol-water 1:1:0.3 121. 
This extract and the lower phase were transferred to aluminium planchets and counted in a gas flow counter. 
The reaction mixture for the direct transfer of glucose from Dol-PGlc to the acceptor containined: 70 mM Tris-maleate, pH 
7.7, 0.18% deoxycholate, 3.5 mM Na-EDTA, 14 mM mercaptoethanol, [ 14C] Dol-P-Glc (2,000 cpm) and an aliquot of the 
isolated fractions containing 0.5 mg of protein, in a final volume of 140 ~1. After incubating for 15 min at 30”, 0.4 ml of 
methanol, 0.6 ml of chloroform and 0.2 ml of 4 mM MgCla were added. After centrifugation both the upper and lower phases 
were discarded and the remaining precipitate was washed again with the same methanol-chloroform-MgCla mixture. The Glc- 
acceptor was then extracted with three 0.5 ml portions of chloroform-methanol-water 1: 1:0.3. The extracts were counted as 
outlined above, In both assays appropriate blanks were made and subtracted. 
Acknowledgements 
This work was supported by grants from the 
Consejo National de Investigaciones CientiEcas y 
TBcnicas (Argentina). NHB and AJP are career in- 
vestigators of this latter institution. 
References 
[l] NH. Behrens and L.F. Leloir, Proc. Natl. Acad. Sci. U.S. 
66 (1970) 15 3. 
[2] N.H. Behrens, A.J. Parodi and L.F. Leloir, Proc. Natl. 
Acad. Sci. U.S. 68 (1971) 1758. 
f 31 A.J. Parodi, N.H. Behrens, L.F. Leloir and M.A. Danker& 
Biochim. Biophys. Acta, in press. 
[4] J.B. Richards, P.J. Evansand F.W. Hemming, Biochem. J. 
124 (1971) 957. 
[S ] N.H. Behrens, A.J. Parodi, L.F. Leloir and C.R. Krisman 
Arch. Biochem. Biophys. 143 (1971) 375. 
[6] CC. Widnelland J.R. Tata, Biochem. J. 92 (1964) 313. 
[7] R. Coleman, R.M. Mitchell, J.B. Fineau and J.N. 
Hawthorne, Biochim. Biophys. Acta 135 (1967) 573. 
[S] D.J. MorrB, R.L. Hamilton, H.H. Mollenhauer, R.W. 
Mahley, W.P. Cunningham, R.D. Cheetman and V.S. 
LeQuire, J. Cell BioI. 44 (1970) 484. 
]9] H. Glaumann and J.L.E. Ericsson, J. Cell Biol. 47 
(1970) 555. 
[lo] G.L. Sottocasa, B. Kuylenstierna, L. Ernster and 
A. Bergstrand, J. Cell Biol. 32 (1967) 415. 
[l l] G. Dallner, Acta Pathol. Microbial. Stand., Suppl. 
(1963) 166. 
f12] A. Bergstrand and C. Dallner, Anal. Biochem. 29 (1969) 
351. 
1131 O.H. Lowry, N.V. Rosebrough, A.L. Farr and R.J. 
Randall, BioL Chem. 193 (1951) 265. 
[ 141 G. Dallner, P. Siekevitz and G.E. Palade, J. Cell Biol. 30 
(1966) 173. 
[15] J. Burgosand R.A. Morton, Biochem. J. 82 (1962) 454. 
317 


Subcellular distribution of dolichol phosphate 

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Subcellular distribution of dolichol phosphate

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