“Whey” proteins of milk of the red (Macropus rufus) and eastern grey (Macropus giganteus) kangaroo

McKenzie, H.A.; Müller, V.; Treacy, George

doi:10.1016/0305-0491(83)90010-x

Cited by 5 publications

(6 citation statements)

References 33 publications

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“…Comparison of the partial sequence of LLP-A with the Atlas of Protein Sequence data base did not reveal homology with the sequence of any known protein. However, comparison of our results with those of McKenzie et al (1983) suggests that the LLP-A of tammar wallaby milk may be homologous with the Zone C proteins of red-and grey-kangaroo milk. Their Mr values and amino acid compositions are similar, and so are the time of first appearance in the milk of LLP-A, at 26 weeks post partum, and of the Zone C protein of the red kangaroo, at 28 weeks.…”

Section: Discussionsupporting

confidence: 47%

“…One of these changes, which has been observed electrophoretically in red (Macropus rufus) and eastern grey (Macropus giganteus) kangaroos, in the tammar wallaby (Macropus eugenii) and in the quokka (Setonix brachyurus), is the appearance of specific whey proteins at late stages of lactation Jordan & Morgan, 1968;Lemon & Poole, 1969;Bell et al, 1980;Green & Renfree, 1982). Very little is known about these proteins, although two of them have been isolated from the milk of red and grey kangaroos and their Mr values and amino acid compositions determined (McKenzie et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

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A novel whey protein synthesized only in late lactation by the mammary gland from the tammar (Macropus eugenii)

Nicholas¹,

Messer²,

Elliott³

et al. 1987

Biochemical Journal

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A major whey protein which appears in milk from the tammar wallaby (Macropus eugenii) only during the second half of lactation (late lactation protein-A, LLP-A) was purified to apparent homogeneity by ion-exchange chromatography and gel filtration. An Mr of 21,600 +/- 2000 was calculated from its amino acid composition. A computer-based comparison of the sequence of the first 69 amino acid residues with the Atlas of Protein Sequence data base showed no significant homology with known proteins. Antiserum to LLP-A was prepared in rabbits, and single radial immunodiffusion was used to measure the amounts of LLP-A in milk during the first 40 weeks of lactation. LLP-A was first detected at 26 weeks; thereafter its concentration increased abruptly, to reach a maximum of 26 g/l at approx. 36 weeks of lactation. Explants prepared from mammary gland biopsies at 20 and 35 weeks of lactation were exposed to [3H]amino acids for 8 h; immunoprecipitation of tissue extracts showed that, whereas the rate of casein synthesis was the same at both stages of lactation, LLP-A was synthesized only by the 35-week mammary gland.

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Section: Discussionsupporting

confidence: 47%

Section: Introductionmentioning

confidence: 99%

A novel whey protein synthesized only in late lactation by the mammary gland from the tammar (Macropus eugenii)

Nicholas¹,

Messer²,

Elliott³

et al. 1987

Biochemical Journal

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“…Recent X-ray crystallographic data il5i show that j3-lactoglobulin and retinol-binding protein folding is similar and model building suggests a binding site for retinol. In order to characterize -lactoglobulin's active site and to gain more insight into evolutionary constraints which have affected /Mactoglobulins and retinol-binding proteins we have sequenced a protein previously isolated by McKenzie et alJ 16] as a major component in the milk of Eastern Grey Kangaroo (Macropus giganteus). While the preliminary studies failed to identify it as /Mactoglobulin, the protein does possess a high degree of homology in segments thought to be involved in binding vitamin A type compounds.…”

Section: Nachweis Von ß-Lactoglobulin In Känguruhmilch Primärstruktumentioning

confidence: 99%

β-Lactoglobulin Identified in Marsupial Milk. The Primary Structure, Binding Site and possible Function of β-Lactoglobulin from Eastern Grey Kangaroo(Macropus giganteus)

Godovac‐Zimmermann¹,

Shaw²

1987

Biological Chemistry Hoppe-Seyler

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0-Lactoglobulin has been isolated in the milk of the Eastern Grey Kangaroo (Macropus giganteus). This is the first time this protein has been reported to be in the milk of marsupials.The complete amino-acid sequence has been determined by spinning cup and pulsed liquid phase microsequencing of the protein and peptides after enzymatic or cyanogen bromide cleavages.The 155-residue protein is the shortest (3-lactoglobulin so far sequenced. When the kangaroo protein is included in a comparison of the members of the 0-lactoglobulin family, the percentage of residues common to all members is reduced from 33% to 13%. Despite the large number of accumulated amino-acid exchanges the protein exists as a dimer and shows higher homology to the usually very conservative dimeric, ruminant 0-lactoglobulins than to the monomeric protein from monogastrics. Half-cystine residues that form disulphide bridges are conserved. The Eastern Grey Kangaroo 0-lactoglobulin possesses significant homology in several characteristic segments thought to be important for a functional trait common to the j3-lactoglobulin family and retinol-binding proteins. Structural similarity to the retinol-binding protein is indicated by 22% of identical residues. Homology to the (3-lactoglobulins and retinolbinding proteins, the binding site and possible function based on comparative structural studies are discussed. Nachweis von ß-Lactoglobulin in Känguruhmilch. Primärstruktur, Bindungsstellen und mögliche Funktion des ß-Lactoglobulins des grauen Riesenkänguruhs (Macropus giganteus)Zusammenfassung: In der Milch des grauen Riesenkänguruh (Macropus giganteus) wurde erstmals ß-Lactoglobulin nachgewiesen und daraus isoliert. Die vollständige Aminosäuresequenz wurde mit automatischer Mikrosequenzierung (spinning cup und pulsed liquid phase) der Kette und der Peptide nach enzymatischer oder Bromcyanspaltung bestimmt. Es ist mit 155 Resten das kürzeste aller bisher sequenzierten ß-Lactoglobuline. Die Einbeziehung dieses ß-Lactoglobulins in den Vergleich vermindert die Homologie innerhalb dieser Proteinfamilie von 33% auf 13% identische Positionen. Trotz der vielen Aminosäureaustausche liegt das Protein als Dimeres vor und zeigt eine größere Homologie zu den sehr konservativen dimeren ß-Lactoglobulinen der Wiederkäuer, als zu den Monomeren der Nichtwiederkäuer. Die Positionen der disulfidbildenden Cysteine sind in der Struktur konserviert. Im ß-Lactoglobulin des grauen Riesenkängu-ruhs findet man signifikante Homologien in

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“…Little is known about putative chemosignalling proteins in marsupials, although a well-developed vomeronasal organ similar to rodents [52][53][54][55] suggests a potential for detection of large chemosignalling molecules that might include proteins. Lipocalin-like proteins are excreted in milk during lactation of the Tamar wallaby [56][57][58], red kangaroo [59], grey kangaroo [59], quokka [60] and the brushtail possum [61], some of which are homologous to marsupial β-lactoglobulins [59,61], and another more closely resembles rodent MUPs [61]. Trichosurin (a MUP-like lipocalin) was the first solved 3D structure of a lipocalin from a metatherian [62] and has been conjectured to bind small phenolic compounds that might prime the neonate liver to produce enzymes required to metabolize toxic plant phenols, reducing dietary limitations [62].…”

Section: Introductionmentioning

confidence: 99%

Vulpeculin: a novel and abundant lipocalin in the urine of the common brushtail possum, Trichosurus vulpecula

et al. 2020

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Lipocalins are a family of secreted proteins. They are capable of binding small lipophilic compounds and have been extensively studied for their role in chemosignalling in rodent urine. Urine of the common brushtail possum ( Trichosurus vulpecula ) contains a prominent glycoprotein of 20 kDa, expressed in both sexes. We have isolated this protein and determined its primary sequence by mass spectrometry, including the use of metabolic labelling to resolve the leucine/isoleucine isobaric ambiguity. The protein sequence was identified as a lipocalin, and phylogenetic analysis grouped the protein with other marsupial lipocalin sequences in a phylogenetic clade distinct from established cross-species lipocalin sub-families. The pattern of expression in possum urine and the similarity in sequence and structure to other lipocalins suggests this protein may have a role in brushtail possum chemosignalling.

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“Whey” proteins of milk of the red (Macropus rufus) and eastern grey (Macropus giganteus) kangaroo

Cited by 5 publications

References 33 publications

A novel whey protein synthesized only in late lactation by the mammary gland from the tammar (Macropus eugenii)

A novel whey protein synthesized only in late lactation by the mammary gland from the tammar (Macropus eugenii)

β-Lactoglobulin Identified in Marsupial Milk. The Primary Structure, Binding Site and possible Function of β-Lactoglobulin from Eastern Grey Kangaroo(Macropus giganteus)

Vulpeculin: a novel and abundant lipocalin in the urine of the common brushtail possum, Trichosurus vulpecula

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