Action of rat liver cathepsin B on bradykinin and on the oxidized insulin A-chain

Rat liver cathepsin B was tested for its peptide-bond specificity against bradykinin and the oxidized insulin A-chain. Bradykinin was shown to be resistant to the action of cathepsin B. One possible reason for this resistance is the proline content of the peptide and the discrimination against proline residues at three or four subsites of cathepsin B. Oxidized insulin A-chain was degraded by a peptidyl dipeptidase activity. Three dipeptides were cleaved from the C-terminal part of the insulin A-chain after having been incubated for 2 h (molar ration E:S = 1:2800) and six dipeptides were released after a longer digestion (10 h, E:S = 1:575).     

The twin-arginine translocation system and its capability for protein secretion in biotechnological protein production

The biotechnological production of recombinant proteins is challenged by processes that decrease the yield, such as protease action, aggregation, or misfolding. Today, the variation of strains and vector systems or the modulation of inducible promoter activities is commonly used to optimize expression systems. Alternatively, aggregation to inclusion bodies may be a desired starting point for protein isolation and refolding. The discovery of the twin-arginine translocation (Tat) system for folded proteins now opens new perspectives because in most cases, the Tat machinery does not allow the passage of unfolded proteins. This feature of the Tat system can be exploited for biotechnological purposes, as expression systems may be developed that ensure a virtually complete folding of a recombinant protein before purification. This review focuses on the characteristics that make recombinant Tat systems attractive for biotechnology and discusses problems and possible solutions for an efficient translocation of folded proteins.     

The N‐Terminal Sequences of Four Major Hydrogenosomal Proteins Are Not Essential for Import into Hydrogenosomes of Trichomonas vaginalis

The human pathogen Trichomonas vaginalis harbors hydrogenosomes, organelles of mitochondrial origin that generate ATP through hydrogen‐producing fermentations. They contain neither genome nor translation machinery, but approximately 500 proteins that are imported from the cytosol. In contrast to well‐studied organelles like Saccharomyces mitochondria, very little is known about how proteins are transported across the two membranes enclosing the hydrogenosomal matrix. Recent studies indicate that—in addition to N‐terminal transit peptides—internal targeting signals might be more common in hydrogenosomes than in mitochondria. To further characterize the extent to which N‐terminal and internal motifs mediate hydrogenosomal protein targeting, we transfected Trichomonas with 24 hemagglutinin (HA) tag fusion constructs, encompassing 13 different hydrogenosomal and cytosolic proteins of the parasite. Hydrogenosomal targeting of these proteins was analyzed by subcellular fractionation and independently by immunofluorescent localization. The investigated proteins include some of the most abundant hydrogenosomal proteins, such as pyruvate ferredoxin oxidoreductase (PFO), which possesses an amino‐terminal targeting signal that is processed on import into hydrogenosomes, but is shown here not to be required for import into hydrogenosomes. Our results demonstrate that the deletion of N‐terminal signals of hydrogenosomal precursors generally has little, if any, influence upon import into hydrogenosomes. Although the necessary and sufficient signals for hydrogenosomal import recognition appear complex, targeting to the organelle is still highly specific, as demonstrated by the finding that six HA‐tagged glycolytic enzymes, highly expressed under the same promoter as other constructs studied here, localized exclusively to the cytosol and did not associate with hydrogenosomes.     

Characteristics of the menstrual cycle in nonhuman primates. II. Ovulation and optimal mating times in macaques.

An analysis of the results of 1,259 limited-duration matings was conducted on colonies of Macaca arctoides and M. fascicularis. Maximum conception occurred at a day of breeding/cycle length (DB/CL) ratio of 0.40--0.41 with a range of DB/CL ratios for successful matings from 0.39 to 0.44. These values are compared with published values for various endocrine parameters equated to cycle length.     

Feinstruktur der Protonephridien von Paromalostomum proceracauda (Plathelminthes,Macrostomida)

Zusammenfassung Die Protonephridien von Paromalostomum proceracauda bestehen aus je einem Terminalkomplex und einem ausleitenden Kanal. Jeder Terminalkomplex setzt sich aus drei multiciliären Terminalzellen mit jeweils separatem Filtrationsapparat zusammen; die Zellen sind gestaffelt hintereinander angeordnet und bilden ein gemeinsames Reusenlumen. Der Nephridialkanal, der nicht an der Ultrafiltration, sondern nur an Resorptionsvorgängen beteiligt ist, besteht aus mindestens zwei röhrenförmigen, hintereinander liegenden ciliären Zellen. Die jeweils letzte Kanalzelle bildet auch den Nephridialporus. Proximal sind die Protonephridien bis zur Basis der Epidermis vollständig von einer interzellulären Matrix umhüllt.

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Fine structure of the protonephridia of Paromalostomum proceracauda (Plathelminthes, Macrostomida)

Summary The protonephridia of Paromalostomum proceracaud consist, respectively, of a terminal complex and a draining canal. Each terminal complex is composed of three multiciliary terminal cells with separate filtration apparatuses; the cells are staggered, forming a joint basket lumen. The nephridial canal consists of two or more tube-shaped ciliary cells, which are arranged in series; these cells do not participate in ultrafiltration but in resorption processes. The last canal cell also forms the nephroporus. Up to the epidermis, the protonephridia are proximally surrounded by an intercellular matrix.

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Abkürzungen cw Cilienwurzel - ep Epidermiszelle - i Interzellularsubstanz - k Kanalzelle - kl Kanallumen - l Leptotrichien - m Muskulatur des Hautmuskelschlauches - n Kern einer Terminaloder Kanalzelle - r Reusenapparat - rl Reusenlumen - rs Reusenstab - t1, 2, 3 Terminalzelle 1, 2, 3 - v Vakuole     

Proacaciberin,A cyanogenic glycoside from Acacia sieberiana var. Woodii

A new cyanogenic glycoside isolated from pods of Acacia sieberiana var. woodii has been shown by chemical and spectroscopic methods to be (2S)-2-[(6-O-α-l-arabinopyranosyl-β-d-glucopyranosyl)oxy]-3-methylbut-3-enenitrileo. Acid-catalysed hydrolysis of the glycoside afforded arabinose and proacacipetalin, and base-catalysed double-bond migration gave 2- [(6-O-α-l-arabinopyranosyl-β- d-glucopyranosyl)oxy ]-3-methylbut-2-enenitrile.     

Ecological Consequences of Animal Migration: Prey Partial Migration Affects Predator Ecology and Prey Communities

Ecosystems - Patterns of animal migration and the ecological forces that shape them have been studied for centuries. Yet ecological impacts caused by the migration, such as altered...