A two-active site one-polypeptide enzyme: the isomaltase from sea lion small intestinal brush-border membrane. Its possible phylogenetic relationship with sucrase-isomaltase.
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The enzyme responsible for all of the isomaltase activity and much of the maltase activity in the small intestine of the Californian sea lion (Zalophus californianus) was isolated by detergent solubilization of the brush-border membrane, followed by immunoadsorption chromatography using antibodies directed against rabbit sucrase-isomaltase. In 0.1% Triton X-100, sea lion isomaltase occurs as a monomer of Mr = 245,000 and is composed of a single polypeptide chain. As judged from the stoichiometry of the covalent binding of the affinity label, conduritol-B-epoxide, this polypeptide chain carries two enzymatically active sites; they are apparently identical and do not show either positive or negative cooperativity. In addition to cross-reacting immunologically with rabbit sucrase-isomaltase, sea lion isomaltase has similar overall enzymatic properties, with the exception of not hydrolyzing sucrose. The Alaskan fur seal (Collarhinus ursinus) has a two-active site isomaltase; however, in contrast to the sea lion, this animal is endowed with a small but significant sucrase activity. Along with (fully active) pro-sucrase-isomaltase, sea lion isomaltase is one of the very few examples of enzymes with more than one active site on a single polypeptide chain acting "in parallel" (rather than "in series"). Furthermore, this enzyme triggers some interesting questions on the phylogenetical pedigree of small intestinal sucrase-isomaltase. (+info)
Luteal regression, follicle growth and the concentration of some plasma steroids during lactation in grey seals (Halichoerus grypus).
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Ovaries of lactating grey seals, which had been shot, were measured to obtain the size of each follicle and corpus luteum. Plasma samples were collected by temporarily immobilizing lactating females. The single corpus luteum regressed rapidly after pupping and circulating progesterone levels declined at parturition and remained low throughout most of lactation. A single wave of follicular growth began about the time of parturition and gave rise to a single mature follicle towards the end of lactation. This coincided with high plasma oestradiol-17 beta concentrations and behavioural oestrus. A corpus luteum inhibited follicular growth in the ipsilateral ovary. The concentration of plasma progesterone increased in some seals late in lactation, indicating that ovulation sometimes occurred before the end of lactation. This was confirmed by observation of ovaries from shot seals. (+info)
Plasma concentrations of oestrone, progesterone and corticosteroids during late pregnancy and after parturition in the harbour seal, Phoca vitulina.
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Blood samples were taken at weekly intervals during the last 2 months of pregnancy from a mature (7-year-old) harbour seal which had conceived and was kept in captivity. The concentrations of oestrone, oestrone sulphate, progesterone and glucocorticoids were determined by radioassays. The plasma levels of unconjugated oestrone were slightly greater than those of oestrone sulphate. Total oestrone declined steadily over the last month from a peak of 2.3 ng/ml at 30 days before parturition. Plasma progesterone concentrations rose to 61 ng/ml at 2 weeks before parturition and fell to about half that value by 2 days before birth of a normal male pup. Plasma glucocorticosteroids reached a peak of 164 ng/ml, also at 2 weeks, but showed only a slight decline thereafter. A higher value (392 ng/ml) was recorded 5 days after parturition. (+info)
Fine structure of Leydig cells in crabeater, leopard and Ross seals.
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Ultrastructural study of the Leydig cells of nonbreeding crabeater, leopard and Ross seals showed that three types of cells could be distinguished. Type I cells possessed the cytological features typical of steroid-secreting cells. Type II cells exhibited various features of degeneration, e.g. accumulation of large amounts of lipofuscin granules (residual bodies), lipid droplets, secondary lysosomes, rectangular crystalloids, and previously undescribed 'peculiar bodies'. These cellular inclusions and debris were released into the interstitium to be phagocytosed by macrophages and/or resorbed by the lymphatics. Type III Leydig cells contained large amounts of lipid droplets, sparse cytoplasmic organelles and essentially became lipid storage cells. (+info)
Characterization of phocid herpesvirus-1 and -2 as putative alpha- and gammaherpesviruses of North American and European pinnipeds.
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To study the relationships between herpesvirus recently isolated from different pinniped species, antigenic and genetic analyses were performed. First, herpesviruses isolated from North American harbour seals (Phoca vitulina), a Californian sea lion (Zalophus californianus) and a European grey seal (Halichoerus grypus) were examined in an enzyme immunoassay (EIA) with a panel of monoclonal antibodies which had previously been shown to allow typing of herpesviruses from European harbour seals into two distinct virus types: phocid herpesvirus type-1 and type-2 (PhHV-1 and PhHV-2). The EIA data showed that all but one of the isolates from seals ranging in United States coastal waters were PhHV-2-like while the European grey seal herpesvirus was PhHV-1-like. Genetic characterization was facilitated by PCR analysis using primers based on conserved regions of the glycoprotein B and D (gB and gD) genes of the antigenically closely related canid (CHV) and felid (FHV) herpesvirus. Specific amplified products were obtained with five isolates antigenically characterized as PhHV-1-like but not with five PhHV-2-like isolates. Sequence analysis of the PCR products confirmed greatest similarity to members of the genus Varicellovirus of the Alphaherpesvirinae and in particular to CHV. Sequence analysis of two EcoRI fragments of the PhHV-2 genome (European isolate 7848) revealed greatest similarity to gammaherpesviruses and in particular equine herpesvirus-2. Although an unambiguous subgrouping was not feasible, this is the first evidence that PhHV-2 may be a putative gammaherpesvirus of pinnipeds. (+info)
Electron microscope observations on a virus transmissible from pinnipeds to swine.
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Evidence from immunological tests and electron microscopy indicates that a virus isolated from an Alaskan fur seal is transmissible to swine. The virus is one of the San Miguel sea lion viruses and a member of the calicivirus groups. (+info)
San Miguel sea lion virus fed to mink and pigs.
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Mink became infected with San Miguel sea lion virus when fed ground meat from seal carcasses showing vesicular-like lesions in the skin. The mink also contracted the infection when they were fed San Miguel sea lion virus infected pig meat or cell culture propagated virus. San Miguel sea lion virus infection in mink was inapparent but the virus was isolated from blood and rectal swabs. Pigs treated similarly with the same virus preparations given to mink developed a severe vesicular disease syndrome similar to that produced by vesicular exanthema of swine. In a separate trial, pigs fed a large sample of commercial ground seal meat did not develop disease signs or antibodies. Further work is needed to assess the hazard of introducing San Miguel sea lion virus into swine on the same premises when potentially San Miguel sea lion virus infective seal meat is fed to mink. (+info)
Single major polypeptide of a calicivirus: characterization by polyacrylamide gel electrophoresis and stabilization of virions by cross-linking with dimethyl suberimidate.
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A calicivirus, San Miguel sea lion virus serotype 4, isolate 15FT, externally labelled with 125I, was shown by gel electrophoresis to possess a single major polypeptide. The polypeptide migrated anomalously upon electrophoresis in two sodium dodecyl sulfate (SDS) systems: more slowly than bovine serum albumin in a continuous phosphate-buffered system and more rapidly than bovine serum albumin in a discontinuous system. Estimated molecular weights in the two systems were approximately 71,000 and 64,000, respectively. There was no clear evidence for a minor virion polypeptide. Treatment of purified San Miguel sea lion virions with dimethyl suberimidate, a cross-linking reagent, preserved virion integrity during long-term storage at 4 degrees C. Oligomeric species of the polypeptide were observed upon electrophoresis of products from cross-linked virions. Based upon a preferred polypeptide molecular weight estimate of 71,000 and distribution of oligomeric species, a calicivirion model with 120 monomeric protein units is proposed as an alternative to a 180-unit model. (+info)