Isolation and characterization of hemagglutinins from the spongeDysidea herbacea

Summary The spongeDysidea herbacea (Keller) was found to possess hemagglutinins. The major component, DHA-I, is a protein with a mol.wt of 26,000, which dissociates into subunits of equal size (14,000). It contains large amounts of glutamic acid and aspartic acid residues, but no half-cystine, methionine or histidine residues. DHA-I reacted with rabbit and human AB0 erythrocytes. D-galactose and lactose were effective inhibitors of DHA-I. The sponge also contained a minor component(s) which reacted preferentially with rabbit erythrocytes but not with human AB0 erythrocytes.Acknowledgment. We thank Dr. M. Yamazaki, Faculty of Pharmaceutical Sciences, Teikyo University, for testing mitogenic activity ofDysidea agglutinins. This study was partly supported by a grant-in-aid for Overseas Scientific Survey from the Ministry of Education, Science and Culture, Japan.     

Isolation of a hexaprenylhydroquinone sulfate from the marine sponge Dysidea sp. as an H,K-ATPase inhibitor

A hexaprenylhydroquinone sulfate has been isolated as an H,K-ATPase inhibitor from a marine sponge Dysidea sp. It also inhibited phospholipase A2 as well as secretion of gastric acid in rats.     

Isolation and characterization of a cystine-containing octapeptide from silk

Zusammenfassung Isolierung und Strukturaufklärung eines Oktapeptides aus Seidenfibroin ausBombyx mori.     

Isolation and partial characterization of cuticular collagen from the parasitic nematodeGaigeria pachyscelis

Summary The cuticle from adultGaigeria pachyscelis was isolated by solubilizing the internal tissues with sodium dodecyl sulphate (SDS) at 37°C. Cuticular protein was extracted with guanidine-HCl and -mercaptoethanol and purified by ammonium sulphate fractionation and DEAE-cellulose chromatography. SDS-polyacrylamide gel electrophoresis of purified protein revealed 2 polypeptides with apparent mol. wts of 58,000 and 74,000. As judged from their hydroxyproline content both of them are collagenous in nature. Results of gel filtration indicate that cuticular collagen exists in two forms, a non-associated form at low concentration and an associated form at high concentration.Acknowledgments. We thank Drs L.N. Singh and H.C. Tewari for providing the necessary facilities. Laboratory assistance of Mr Ram Kishore is highly appreciated.     

Isolation and characterization of a new hemagglutinin from the red algaGracilaria bursa-pastoris

Summary A new agglutinin has been isolated from the red algaGracilaria bursa-pastoris by affinity chromatography on a yeast mannan-Cellulofine column. This agglutinin was isolated as a monomeric glycoprotein with a relatively low molecular weight. It had an isoelectric point of 4.7 and contained large amounts of Gly, Asx and Glx. It agglutinated trypsin-treated rabbit erythrocytes at the low concentration of 30 ng/ml. The activity was inhibited only by glycoproteins bearing N-glycans. This agglutinin also showed mitogenic activity for mouse splenic lymphocytes.     

Isolation and characterization of a high-molecular-weight glycoprotein from the endometrium of porcine uteri

Summary A novel glycoprotein was isolated from the endometrium of porcine uteri. This high-molecular-weight glycoprotein consisted of 25% of protein and 73% of carbohydrate. The carbohydrate composition was quite characteristic in that equimolar N-acetylglucosamine and galactose were major constituents. Its unique nature makes it distinguishable from hitherto-reported glycoproteins.     

Isolation and characterization of a high-molecular-weight glycoprotein from the endometrium of porcine uteri

A novel glycoprotein was isolated from the endometrium of porcine uteri. This high-molecular-weight glycoprotein consisted of 25% of protein and 73% of carbohydrate. The carbohydrate composition was quite characteristic in that equimolar N-acetylglucosamine and galactose were major constituents. Its unique nature makes it distinguishable from hitherto-reported glycoproteins.     

Isolation and characterization of hallachrome,a red pigment from the sea wormHallaparthenopeia

Riassunto Viene descritto l'isolamento e la caratterizzazione dello Hallacromo, il pigmento epiteliale del verme marinoHalla parthenopeia che è stato oggeto di numerose ricerche fin dal 1931. Sulla base dei risultati ottenuti si può concludere che il pigmento, contrariamente a quanto riportato da altri Autori, è un metilmetossi-ossi-1, 2-antrachinone (I). Sono in corso ulteriori ricerche per giungere alla definizione completa della struttura del pigmento, che è il primo antrachinone rinvenuto in natura non sostituito nelle posizioni 9 e 10.

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This investigation was supported by a grant from Laboratorio per la Chimica e Fisica di Molecole di Interesse Biologico del C.N.R., Napoli.     

Isolation and characterization of a new hemagglutinin from the red alga Gracilaria bursa-pastoris

A new agglutinin has been isolated from the red alga Gracilaria bursa-pastoris by affinity chromatography on a yeast mannan-Cellulofine column. This agglutinin was isolated as a monomeric glycoprotein with a relatively low molecular weight. It had an isoelectric point of 4.7 and contained large amounts of Gly, Asx and Glx. It agglutinated trypsin-treated rabbit erythrocytes at the low concentration of 30 ng/ml. The activity was inhibited only by glycoproteins bearing N-glycans. This agglutinin also showed mitogenic activity for mouse splenic lymphocytes.     

Minor sesquiterpenoids from the sponge Axinella cannabina

Summary On the basis of chemical and spectral evidence, the structureIV has been assigned to Axisonitrile-4, an axane-sesquiterpenoid isonitrile, isolated from the spongeAxinella cannabina; in the same organism have been also found Axisothiocyanate-4 (V) and Axammide-4 (VI).This investigation was supported by a grant of the Consiglio Nazionale delle Ricerche, Rome (NA 75.00770.03).     

Isolation and partial characterization of ovine lactoferrin

Summary Ovine lactoferrin was isolated by ammonium sulfate precipitation and ion exchange chromatography. Comparative analyses were performed with the bovine protein. Differences in the amino acid compositions and the tertiary structure of the proteins were observed.Acknowledgments. We would like to thank Dr M. Casey for his interest in this work, Dr P. Lavanchy for performing the amino acid analyses and M.F. Baumann for providing us with ewe milk.     

Isolation and partial characterization of a phytotoxic glycoprotein from culture filtrates ofRhynchosporium secalis

Summary Rhynchosporium secalis (Oud.) Davis produces a phytotoxic compound with a mol. wt of 275×10³ which is able to induce chlorotic symptoms in both susceptible and resistant barley leaves. Collectively, the data suggest that the toxin is a glycoprotein. Mild base treatment, by elimination, indicates that threonine and serine are involved in o-glycosidic linkages with the carbohydrate moiety. Sugar residues occur in the molecule in the ratio of mannose, rhammnose, galactose, glucosamine 13.6111.Acknowledgments. We acknowledge the assistance of Mr M. McNeil and P. Albersheim in doing the sugar analyses shown in this report. Financial support for this project was provided by a BARD grant 1-31-79, the French government, and the Montana Ag. Expt. Station.     

Isolation and partial characterization of ovine lactoferrin.

Ovine lactoferrin was isolated by ammonium sulfate precipitation and ion exchange chromatography. Comparative analyses were performed with the bovine protein. Differences in the amino acid compositions and the tertiary structure of the proteins were observed.     

Isolation and partial characterization of the moult-inhibiting hormone of the crustacean eyestalk

Résumé Un fragment soluble dans le phénol de pédoncule oculaire du CrabeOcypode macrocera a, sur la mue, un effet inhibitif prononcé. Cette inhibition est sans effet sur les chromatophores et sur l'absorption de l'eau pendant la pré-mue du crabe. L'hormone est soluble dans l'éthanol, le méthanol et le phénol et inactivée par la trypsine. L'hormone d'inhibition de la mue paraît être une peptide.     

Isolation of an antifreeze peptide from the Antarctic sponge <Emphasis Type="Italic">Homaxinella balfourensis</Emphasis>

Polar plants and animals survive in subzero waters (-2 degrees C) and many of these marine organisms produce antifreeze proteins (AFPs) to better adapt themselves to these conditions. AFPs prevent the growth of ice crystals which disrupt cellular membranes and destroy cells by inhibiting crystallization of water within the organism. The hydrophilic extract of an Antarctic sponge Homaxinella balfourensis exhibited a non-colligative freezing point depression effect on the crystal morphology of water. The extract was purified by repeated reverse phase high-pressure liquid chromatography, then assayed and shown to contain several AFPs. The major peptide was isolated, analyzed using matrix-assisted laser desorption ionization mass spectrometry and the partial structure of the peptide identified through amino acid sequencing. AFPs have potential applications in agriculture, medicine and the food industry.     

The lectins fromAgaricus edulis. Isolation and characterization

Summary 2 lectins from the mushroomAgaricus edulis were isolated, after heating the crude extract at 75°C, by ion exchange chromatography and gel chromatography using QAE-Sephadex A-50 and Sephadex G₇₅. Some hemagglutinating and physicochemical properties of the agglutinins are reported.