Vol. 253, No. Ii, Issue of September 10, pp.

6086-6091, 1978
Printed m U.S.A.

The Sugar Chain Structures of ABO Blood Group Active Glycoproteins

Obtained from Human Erythrocyte Membrane*
(Received for publication, January 18, 1978)

Seiichi Takasaki, Katsuko Yamashita, and Akira Kobata

From the Department of Biochemistry, Kobe University School of Medicine, Ikuta-ku, Kobe, Japan

The glycoproteins of human erythrocyte membrane sugar chains of membrane and extracellular glycoproteins.
have two groups of sugar chains with blood type ABH This paper describes the isolation and structural studies of
determinants, which are quite distinct in their molec- the sugar moieties of the human erythrocyte glycoproteins
ular sizes. with blood group H determinants.
A neutral sugar chain and an acidic sugar chain,
which belong to the small size group, were isolated EXPERIMENTAL PROCEDURES’
from the glycoproteins obtained from the erythrocyte
RESULTS
of blood type 0 individuals, and their structures were
elucidated as Fucal 4 2GaljIl -+ 3Nacetylgalactos-
aminitol and Fucal + 2Galfil + B(AcNeua2 + 6)N- Neutral Sugar Chains with H Blood Group Determinant
acetylgalactosaminitol, respectively. The molecular Estimation of Molecular Weight of Blood Group H Active
weight of the large sugar chains with ABH determi- Oligosaccharides Labeled with N-f4C]Acetylgalactosa-
nants were estimated to be more than 4000. mine-The radioactive glycoproteins, prepared from blood
Both large and small neutral sugar chains of mem- group 0 erythrocyte glycoproteins by incubating with UDP-
brane glycoproteins obtained from blood type 0 eryth- N-[“‘C]acetylgalactosamine and Al-enzyme, were subjected to
rocyte could serve as acceptors of a-N-acetylgalacto- alkaline degradation. When the radioactive degradation prod-
saminyltransferases purified from milk of blood type uct was first subjected to paper electrophoresis at pH 5.4, the
A1 and AZ individuals, producing the same radioactive radioactivity was detected in the neutral sugar region, but not
sugar chain distribution patterns. However, the acidic in the glycopeptide region, nor in any acidic sugar region (data
sugar chain with the H determinant could not serve as
not shown). This neutral oligosaccharide fraction was ex-
an acceptor of these enzymes.
tracted from paper with water, and was then analyzed by gel
filtration on Bio-Gel P-4. As shown in Fig. lA,’ the radioactive
oligosaccharides were separated into two peaks. One was a
Evidence that the complex carbohydrates in plasma mem- large oligosaccharide eluted in the void volume fraction, the
branes are functionally related to various cell surface recog- size of which was larger than a glucose polymer composed of
nition phenomena is accumulating (1-13). However, the infor- 20 glucose units, and another was a small oligosaccharide
mation about the structures of the sugar chains in plasma included in the gel, the size of which was nearly equal to a
membrane glycoproteins is scanty as compared to those in glucose polymer composed of 6 glucose units.
extracellular glycoproteins. In the case of an ovarian cyst mucin, the radioactive sugar
Thomas and Winzler (14) elucidated the structure of the pattern was very different, showing wider distribution in size
major serine- and threonine-linked tetrasaccharide of the of the sugar chains with the blood group determinant (Fig.
human erythrocyte membrane glycoproteins as AcNeucu2 + 1B).
3GalPl + 3(AcNeua2 -+ 6)GalNAc. Two inconsistent struc- In this gel filtration, 1 residue of N-acetylhexosamine be-
tures of the asparagine-linked sugar chains of erythrocyte haves almost as 2 hexose units.” Since the small blood group
membrane glycoproteins were presented by Kornfeld and A active oligosaccharide contains 1 mol each of N-acetylga-
Kornfeld (10) and Thomas and Winzler (15). lactosamine in its nonreducing and reducing terminals (see
By using an cu-N-acetylgalactosaminyltransferase (A-en- below), its size was estimated as tetrasaccharide. The large
zyme) which transfers IV-acetylgalactosamine from UDP-N- radioactive oligosaccharide was excluded from Bio-Gel P-4,
acetylgalactosamine to the C-3 position of the galactose resi- but was included in Bio-Gel P-10 and was eluted with a
due of the only H antigenic determinant, Fucnl + 2Ga1, the relatively sharp peak as shown in Fig. 2A. We also examined
occurrence of H antigenic determinants in human erythrocyte the radioactive sugar pattern of blood group A active eryth-
membrane glycoproteins was found (16). Since the structures rocyte membrane glycoproteins prepared by using Al-enzyme.
of the sugar chains with ABH blood group determinants were The elution pattern from Bio-Gel P-4 (data not shown) and
well studied with ovarian cyst glycoproteins, these erythrocyte from Bio-Gel P-10 columns (Fig. 2B) was the same as that of
membrane glycoproteins are useful materials to compare the the Al-enzyme product. Therefore, erythrocyte glycoproteins
showed a very characteristic and simple sugar pattern in
* This work was supported in part by research grants from Toray
Science Foundation and Scientific Research Fund Grant 201554 of
the Ministry of Education, Science and Culture of Japan. This paper ’ Portions 3f this paper (including “Experimental Procedures” and
is a part of the dissertation submitted by S. T. to Kobe University Figs. 1 to 12) are presented in a miniprint at the end of this paper.
School of Medicine for the degree requirement of Doctor of Medical Full size photocopies are available from the Journal of Biological
Sciences. The costs of publication of this article were defrayed in part Chemistry, 9650 Rockville Pike, Bethesda, Md. 20014. Request Doc-
by the payment of page charges. This article must therefore be hereby ument No. 78M-82, cite author(s) and include a check or money order
marked “aduertisement” in accordance with 18 U.S.C. Section 1734 for $2.25 per set of photocopies.
solely to indicate this fact. ’ T. Mizuochi, K. Yamashita, and A. Kobata, unpublished data.

6086

This is an Open Access article under the CC BY license.

 Oligosaccharides of Membrane Blood Group Glycoprotein 6087

contrast to ovarian cyst mucin. In order to study the structure the Reducing Terminal-Alkaline degradation of glycopro-
of the small blood type A oligosaccharide, a substantial tein (50 mg) from blood type 0 erythrocyte was performed in
amount of it was isolated from the glycoprotein obtained from the presence of NaB:‘H4. The neutral oligosaccharides in the
the membrane of the blood type A1 erythrocyte by using the degradation product were separated by paper electrophoresis
N-[‘4C]acetylgalactosamine-labeled oligosaccharides as stan- at pH 5.4, and were subjected to paper chromatography for 7
dard. days using Solvent II. The small blood type H oligosaccharide
Isolation of Blood Type A Oligosaccharides Labeled at having the same mobility as tritium-labeled triitol (Fig. 4B)
the Reducing Terminal-Alkaline degradation of glycopro- was extracted from paper with water, and was further purified
teins (5 mg) obtained from blood type A erythrocyte was by rechromatography using the same solvent. Using the spe-
performed in the presence of NaB”H4 to release the O-glycos- cific activity of NaB”H4, the yield of the triitol was calculated
idically linked sugar chains as radioactive oligosaccharides as 80 nmol.
labeled at the reducing terminal. Methylation Study of the Blood Type H Oligosaccha-
The degradation product was fist subjected to paper elec- ride-The permethylated product of the blood type H oligo-
trophoresis at pH 5.4 (data not shown). Since the radioactive saccharide was prepared as described under “Experimental
blood type A oligosaccharides obtained from the radioactive Procedures” and was analyzed by gas-liquid chromatography.
glycoproteins by A-enzyme action were neutral, as already As shown in Fig. 7B, a major peak (Peak 0 was detected with
described, the tritium-labeled oligosaccharides, migrating at a minor contaminating disaccharide peak (Peak 14. Peak I
the neutral region, were extracted from paper with water, was further subjected to mass spectrometric analysis (Fig.
concentrated, and then subjected to paper chromatography 7C). The fragment ion, m/e 133, specific for C-3-linked N-
using Solvent I (Fig. 3A). In this chromatography, the large acetylgalactosaminitol, was detected, but the other fragment
blood group oligosaccharide remained at the origin, and the ions, m/e 218, 262, which are specific for C-&linked N-acetyl-
small one migrated with the R z filcoiV~~,,~tlt~,l
,. value of 0.71 (Fig. galactosaminitol, and m/e 174, specific for C-4- or C-&linked
3B). After water extraction, the tritium-labeled small blood N-acetylgalactosaminitol, were not detected. This result is
group oligosaccharide, which was underlined in Fig. 3A, was consistent with that obtained from the periodate oxidation
further purified by paper chromatography using Solvents I study.
and II. About 11 nmol of the tritium-labeled oligosaccharide, Based on these data, the structure of the neutral blood type
as calculated on the basis of the specific activity of NaB”H4 H trisaccharide was proposed as Fucal + 2Gal/?l --, 3N-
used, was obtained. acetylgalactosaminitol.
Sequence Analysis-The isolated tritium-labeled small ol-
igosaccharide was first digested with a-N-acetylgalactosamin- Acidic Blood Group Active Oligosaccharide
idase from beef liver and was analyzed by paper chromatog- Presence of Acidic Blood Group Active Oligosaccha-
raphy using Solvent II. The digested product moved faster ride-The core disaccharide, GalPl + 3GalNAc, of the neu-
than the original oligosaccharide, showing that N-acetylgalac- tral small blood group active sugar chain is also the core of
tosamine was released (Fig. 4B), and this was further con- the major sialosugar chain of human erythrocyte glycopro-
verted to a smaller radioactive oligosaccharide with the same teins reported by Thomas and Winzler (14). Since a sialyl
mobility as Galpl -+ 3N-acetylgalactosaminitol by digestion derivative of blood type H sugar chain was found in pig
with a-fucosidase from Bacillus fulminans, which cleaves submaxillary mucin (30), it is quite possible that blood type H
only Fucal -+ 2Gal linkage (Fig. 4C). sugar chain with sialic acid also occurs in human erythrocyte
This radioactive disaccharide was hydrolyzed by heating in membrane glycoproteins. However, this type of sugar chain
4 N HCl at 100°C for 3 h, and the hydrolysate was subjected cannot be detected by the method using A-enzyme since the
to paper electrophoresis in borate buffer, pH 9.5, after N- enzyme cannot use the sialo-oligosaccharides with H antigenic
acetylation as described under “Experimental Procedures.” determinant as acceptor (31). Therefore, we tried to isolate
As shown in Fig. 5, only radioactive N-acetylgalactosaminitol the acidic oligosaccharide with H antigenic determinant from
was detected. This result shows that the reducing terminal the alkaline NaB”H4 degradation product of glycoproteins
sugar residue of the small blood group oligosaccharide is N- obtained from blood type 0 erythrocyte.
acetylgalactosamine. The alkaline degradation product was subjected to paper
Periodate Oxidation Study-Based on the result of the electrophoresis at pH 5.4 (Fig. 8). Acidic Fractions I and II
sequence analysis and the substrate specificity of A-enzyme, corresponded to disialyl and monosialyl forms of Gal-N-ace-
which transfers N-acetylgalactosamine to Fucnl + 2Gal--- tylgalactosaminitol. An acidic Fraction III, which was ex-
structure producing blood group A determinant (29), the pected to contain the acidic H antigenic oligosaccharide, was
structure of the small blood group oligosaccharide is proposed extracted with water, concentrated, and then digested with
as GalNAcal + 3(Fucal -+ 2)Gal-+ N-acetylgalactosamini- neuraminidase from Clostridium perfringens. When the di-
tol. The linkage of galactose to the reducing terminal N- gest was then subjected to paper chromatography using Sol-
acetylgalactosaminitol was analyzed as follows. vent II, a portion of the radioactivity was detected in the
The radioactive disaccharide, prepared from the blood type region corresponding to H active trisaccharide, and this frac-
A tetrasaccharide by digesting with Lu-N-acetylgalactosamini- tion was further converted to disaccharide with the same
dase and a-L-fucosidase, was subjected to periodate oxidation mobility as Gal/?1 + 3N-acetylgalactosaminitol by Bacillus
as described under “Experimental Procedures.” The reaction fucosidase digestion (data not shown). The structure of this
product was analyzed by paper chromatography using Solvent disaccharide was further identified as GalPl + 3N-acetylga-
II. Radioactive 2-deoxy-2-acetamidothreitol, 2-deoxy-2-ace- lactosaminitol by reducing terminal analysis and periodate
tamidoarabinitol, and 2-acetamidopropanediol, should be the- oxidation as shown in the case of the study of the neutral
oretically produced from C-3-, C-4-, and C&linked N-acetyl- blood group active oligosaccharide. These results obviously
galactosaminitol, respectively. As shown in Fig. 6A, a single indicated the existence of sialic acid containing sugar chain
radioactive peak corresponding to 2-deoxy-2-acetamidothrei- with blood type H determinant.
to1 was detected. This result shows that the galactose residue The approximate amount of the acidic blood type H deter-
attaches to the N-acetylgalactosaminitol by 1 -+ 3 linkage. minant in the glycoprotein was estimated as 0.72 nmol/mg of
Isolation of a Blood Type H Oligosaccharide Labeled at glycoprotein, by using the specific activity of NaB”H+
6088 Oligosaccharides of Membrane Blood Group Glycoprotein

Linkage of Sialic Acid-The linkage of sialic acid in the The large blood group active sugar chain of erythrocyte
acidic H hapten was determined as follows. membrane glycoproteins has a very high molecular weight.
Sialic acid-labeled oligosaccharides, which were prepared Recently, Koscielak et al. (36) reported the occurrence of
by alkaline degradation of sialic acid-labeled glycoprotein as extremely large glycolipids in human erythrocyte membrane
described under “Experimental Procedures,” were used for and named them as megaloglycolipids. Since these glycolipids
this purpose. The electrophoretogram of the alkaline degra- were reported to have blood types A, H, and I activities, care
dation product was qualitatively similar to that shown in Fig. must be taken for the origin of the large blood group active
8A, except that almost negative radioactivity was detected in sugar chains. By the alkaline borohydride treatment, all the
the neutral sugar region (Fig. 8B). This shows that the sialic N-[‘%]acetylgalactosamine, incorporated into human eryth-
acid portions of oligosaccharides were selectively labeled with rocyte membrane glycoproteins by the action of A-enzyme,
tritium. was liberated as a mixture of oligosaccharides. Since glyco-
The region corresponding to monosialyl tri- and tetrasac- sphingolipids, including the megaloglycolipids, are known to
charides, which was underlined in Fig. BB, was extracted with be alkali-stable, the possibility of the contamination of any
water, and was then digested with Bacillus a-L-fucosidase. blood group active glycolipids in our radioactive glycoprotein
The digest was analyzed by paper electrophoresis at pH 5.4. preparation can be eliminated. That all the radioactivity is
As shown in Fig. 8C, only a portion was converted to the linked to glycoproteins was also confirmed by the following
radioactive component migrating as monosialyl disaccharide. experiment. The radioactive glycoprotein was exhaustively
This radioactive monosialyl disaccharide should be derived digested with pronase, and the digest was examined by gel
from the expected acidic H hapten, since the fucosidase re- filtration. As shown in Fig. 12, most of the radioactivity shifted
leases fucose residue only from H antigenic determinants. to lower molecular weight regions. Based on these results, it
Therefore, it was recovered from paper by water extraction was concluded that both small and large blood group active
and was subjected to paper chromatography using Solvent oligosaccharides were derived from glycoproteins, but not
III. As shown in Fig. 9, it showed the same mobility as Gala1 from glycolipids.
+ 3(C;-AcNeua2 + 6)N-acetylgalactosaminitol, but not as Hakomori’s group (37) reported that the membrane of blood
C;-AcNeucu2 + 3Galpl + 3N-acetylgalactosaminitol. This type A, erythrocyte contained three variants of glycolipids
result suggests that sialic acid attaches to N-acetylgalactosa- with branched sugar chains, one of which was missing or
minitol by 2 + 6 linkage. That the sialyl residue is linked at decreased in A2 erythrocytes. The fact that the A,- and AZ-
the C-6 position of N-acetylgalactosamine was further con- enzymes in serum gave different characteristics was also re-
firmed by the following acetolysis study. Acetolysis of this ported by Schachter et al. (38). These results gave rise to the
defucosylated trisaccharide was performed as described under possibility that only Al-enzyme may react with some of the
“Experimental Procedures.” The acetolysis product was ana- sugar chains, producing Al-specific structures. Therefore, pre-
lyzed by paper chromatography. As shown in Fig. 10, the liminary investigation was performed to find out any differ-
mobility of the radioactive sialic acid containing disaccharide ences between the products of A,- and A?-enzymes. The
was the same as CT-AcNeucu2 + GN-acetylgalactosaminitol, maximum amount of N-[‘%]acetylgalactosamine transferred
but not as CT-AcNeun2 + 6Gal. Furthermore, this acetolysis from UDP-N-[‘4C]acetylgalactosamine to H active glycopro-
product was different from CT-GlyNeucu2 -+ GN-acetylgalac- teins by both enzymes was almost equal. The oligosaccharides
tosaminitol, and the sample prior to acetolysis was also differ- liberated by alkaline degradation of the labeled glycoproteins
ent from Gala1 ---) 3(C;-GlyNeucu2 + G)N-acetylgalactosamin- also gave the same gel filtration patterns (Figs. 1 and 2).
itol as shown in Fig. 9. Therefore, we concluded that no marked difference was ob-
From these results, the structure of the acidic H antigenic served between the products of two enzymes. However, the
oligosaccharide was proposed as Fuc~vl -+ 2GalPl + possibility that minor differences of size, which cannot be
3(AcNeucu2 -+ 6)N-acetylgalactosaminitol. detected by our present experiment and of linkage which may
exist in the large sugar chains, still remains. The kinetic
DISCUSSION differences of both A-enzymes in the reaction with glycopro-
Presence of two groups of sugar chains with blood type teins must also be studied.
ABH determinants, which are quite distinct in their molecular Previously, we used the endo-/?-galactosidase of Diplococ-
sizes, was confirmed. The structures of two sugar chains which cus pneumoniae for the structural characterization of the
fall into the smaller group were proposed as shown in Fig. 11. carbohydrate moieties of blood group active glycoproteins
These structures are similar to those of blood group active (16). This enzyme cleaves trisaccharides only from blood
sugar chains in pig submaxillary mucin reported by Carlson group determinants A and B composed of type 2 chain, and
(30), except that the sialic acid residue is N-acetylneuraminic not from those composed of type 1 chain (20). Based on the
acid instead of N-glycolylneuraminic acid. result that N-[“Clacetylgalactosamine, incorporated into the
Both sugar chains have a common disaccharide core, GalPl erythrocyte membrane glycoproteins by A-enzyme action, was
+ 3GalNAc. This disaccharide was also reported by Thomas completely released as a trisaccharide by this enzyme, we
and Winzler (14) as the core portion of sialic acid-containing suggested that blood group active sugar chains of erythrocyte
tetrasaccharide, which is the major 0-glycosidically linked glycoproteins are composed only of type 2 chain. However,
oligosaccharide of human erythrocyte membrane glycopro- the structure of small blood group active sugar chain (A) in
teins. Therefore, these two series of sugar chains are sharing Fig. 11 indicates that the enzyme also acts on GalNAcnl + 3
a common precursor and their relative amount in membrane (Fuccul + 2) GalPl + 3 GalNAc + protein structure. So we
glycoproteins might be regulated by the relative amount of must keep this point in mind in the determination of type 1
the fucosyltransferase and the dialyltransferases in the Golgi and type 2 chain nature of the blood type A and B determi-
membrane of hematopoietic cells. GalPI + 3GalNAc grouping nants.
linked either to serine or to threonine residue is widely dis-
Acknowledgment-We are grateful to Miss J. Fujii for expert
tributed in many glycoproteins (32-35). The results in this secretarial assistance.
paper indicate that these disaccharide groupings can be con-
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6090 Oligosaccharides of Membrane Blood Group Glycoprotein
Oligosaccharides of Membrane Blood Group Glycoprotein 6091