The products of pronase digestion of purified blood group-specific glycoproteins

Donald, A.S.R.

doi:10.1016/0005-2795(73)90235-3

Cited by 72 publications

(57 citation statements)

References 22 publications

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“…The difference is further illustrated by the observation that the ovarian cyst material is alkali labile (Donald 1973). The alkali stability of our material is also in contrast to the BSM found to be alkali labile both in the present control experiments and in previous investigations (reviewed by Gottschalk et al 1972b).…”

Section: Discussioncontrasting

confidence: 66%

“…In the present communication, the amino Accepted 1 l.xii.74 14* acid composition of salivary blood-group substance from donors of blood-group status A and B was investigated. A study of the carbohydrate-protein linkage was performed, as pilot investigations indicated that it is alkali stable (Sonju & Rolla 1971) and thus presumably different from the 0-glycosidic linkage of the cyst material (Donald 1973).…”

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confidence: 99%

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Further Studies of the Chemistry of a Human Salivary Blood‐group Substance

Sønju

Rölla

1975

Acta Pathologica Microbiologica Scandinavica Section C Immunolo

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Sonju, T. & Rolla, G. Further studies of the chemistry of a human salivary blood-group substance. Acta path. rnicrobiol. scand. Sect. C, 83: [215][216][217][218][219][220] 1975.A glycoprotein possessing blood-group and virus haemagglutination inhibition activity was isolated from the saliva of donors of blood groups A and B. T h e glycoprotein was subjected to amino acid analysis and tested for alkali stability and the presence of sulphate. No definite differences in the amino acid composition between the blood groups A and B could be found. T h e salivary glycoprotein was alkali stable and contained a substantial amount of sulphate. T h e results were compared with reported properties of blood-group substances obtained from erythrocytes and ovarian cyst material.

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Section: Discussioncontrasting

confidence: 66%

mentioning

confidence: 99%

Further Studies of the Chemistry of a Human Salivary Blood‐group Substance

Sønju

Rölla

1975

Acta Pathologica Microbiologica Scandinavica Section C Immunolo

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“…Regions of the peptide backbone whieh are not glycosylated are said to be "naked" and henee more vulnerable to proteolysis (Masson 1972). Studies from our laboratory (Hatton et al 1981) as well as others (Donald 1973, Feldhof et al 1979 have indicated that naked regions contain much of the cysteinyl residues and hydrophobic amino acids. The biased distribution of these amino aeids eould lead to localized regions of unique function.…”

Section: / Chemical Composition and Structure Of Mucinmentioning

confidence: 65%

Role of salivary mucins in the protection of the oral cavity

Tabak

Levine

Mandel

et al. 1982

J Oral Pathology Medicine

472

263

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Mucins are the principal organic constituents of mucus, the slimy visco‐elastic material that coats all mucosal surfaces. Compelling evidence suggests that they play an integral role in non‐immune protection of the oral cavity. Specific protective functions include: 1) protection against desiccation and environmental insult, 2) lubrication, and 3) antimicrobial effects against potential pathogens. Biosynthesis of mucin is regulated by both intrinsic (“cooperative sequential specificity”) and extrinsic (“structural modulation”) controls. These controls form the basis by which mucin's structure can be modified to meet a dynamically changing biological need.

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“…The cells was washed and resuspended in ice-cold distilled water, broken by passage twice through a French press at 135 MPa and 4 "C, made 5 % (w/v) in trichloroacetic acid and held in crushed ice for 1 h. The supernatant recovered by centrifugation at 30000 g for 1 h at 4 "C was extracted three times with an equal volume of ether (to remove trichloroacetic acid) and then freeze-dried. The amounts of the pool amino acids were determined using an automated amino acid analyser (Locarte, London) with the buffer system described by Donald (1973). Serine, glutamine and asparagine have identical retention times in this system and so were not separated.…”

Section: Methodsmentioning

confidence: 99%

Uptake of Leucine and Tyrosine and Their Intracellular Pools in Chlorella fusca var. vacuolata

Richards

Thurston

1980

Microbiology

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Chlorella fusca var. vacuolata has high affinity active transport systems for the amino acids L-leucine and L-tyrosine. Leucine at 0.2 ,UM was concentrated at least 222-fold and tyrosine 920-fold. Neither uptake process was inhibited by high concentrations of serine, threonine or phenylalanine. The concentration giving half-maximum rate of uptake was 2.5 ,UM for leucine with a smaller value for tyrosine. The maximum uptake rate for leucine was 10 am01 cell-l min-l. Uptake of leucine and tyrosine was not inhibited by 0.2 m~-2,4-dinitrophenol, which completely inhibited the incorporation of radioactive leucine and tyrosine into protein. Intracellular radioactive leucine did not exchange with an excess of unlabelled leucine added to the medium, except during nitrogen starvation, and only partial exchange occurred with tyrosine. The apparent overall pool size for these amino acids was dependent upon the growth state of the algal cells. The kinetics of incorporation of radioactive amino acids from intracellular pools into protein suggested that both leucine and tyrosine occupied at least two distinct pools within the cells. Tyrosine and methionine were present in smallest amounts (38 and 37 amol cell-l, respectively). Leucine was present at 90 amol cell-l. At least 11 amino acids had higher pool concentrations than leucine, whilst only alanine and glycine were more abundant than leucine in C. fusca protein.

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The products of pronase digestion of purified blood group-specific glycoproteins

Cited by 72 publications

References 22 publications

Further Studies of the Chemistry of a Human Salivary Blood‐group Substance

Further Studies of the Chemistry of a Human Salivary Blood‐group Substance

Role of salivary mucins in the protection of the oral cavity

Uptake of Leucine and Tyrosine and Their Intracellular Pools in Chlorella fusca var. vacuolata

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