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Dive into the research topics where Stefan Kappeler is active.

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Featured researches published by Stefan Kappeler.


Plant Physiology | 1994

Circadian Oscillations of a Transcript Encoding a Germin-Like Protein That Is Associated with Cell Walls in Young Leaves of the Long-Day Plant Sinapis alba L

Christian Heintzen; Ruth Fischer; Slegbert Melzer; Stefan Kappeler; Klaus Apel; Dorothee Staiger

As part of an attempt to analyze rhythmic phenomena in the long-day plant Sinapis alba L. at the molecular level, we have searched for mRNAs whose concentration varies as a function of time of day. Differential screening of a cDNA library established from mRNAs expressed at the end of the daily light phase with probes representing transcripts expressed predominantly in the morning or evening has identified one major transcript. The cDNA, Saglp, encodes a predicted 22-kD protein with an N-terminal signal sequence. The protein shows homology to germin, a protein expressed in wheat embryos after onset of germination. The Saglp mRNA level undergoes circadian oscillations in light/dark cycles with maxima between 8 and 12 PM (zeitgeber time [zt] 12-zt16) and minima around 8 AM (zt0). In plants grown from seed in constant light, transcript levels are constitutive. In constant light regular temperature shifts function as an alternative “zeitgeber” to initiate Saglp transcript oscillations. At the cellular level, Saglp transcripts are expressed in the epidermis and spongy parenchyma of young leaves, and in distinct regions of the epidermis and the cortex in stems and petioles. Strong signals are observed in these tissues around zt12, whereas little expression is found around zt20, suggesting that the underlying oscillatory mechanism(s) operate(s) synchronously in different plant organs. The SaGLP steady-state protein concentration remains constant over light/dark cycles. Immunogold labeling shows that the SaGLP protein is associated with primary cell walls.


Planta | 1994

The proteins encoded by two tapetum-specific transcripts, Satap35 and Satap44, from Sinipis alba L. are localized in the exine cell wall layer of developing microspores

Dorothee Staiger; Stefan Kappeler; Martin Müller; Klaus Apel

By differential screening of a copy DNA (cDNA) library from flowering Sinapis alba L. apices against cDNAs from vegetative apices, two cDNA clones were isolated representing transcripts that are expressed transiently at an early stage of tapetum development. The Satap35 cDNA encodes a polypeptide with a predicted molecular weight of 12.7 kDa and an isoelectric point of 10.4. The Satap44 cDNA codes for a putative 12.4-kDa polypeptide with an isoelectric point of 7.5. The deduced amino-acid sequences display 76% sequence identity and contain an N-terminal stretch of hydrophobic amino acids which has characteristics of secretory signal sequences. In-vitro transcription of the cDNAs and translation of the resulting RNAs in the presence of canine pancreatic microsomes demonstrates that the two proteins are translocated into the microsomes and that the putative preproteins are proteolytically processed to the mature forms. By immunoelectron microscopy the SaTAP35 and SaTAP44 proteins were detected at the developing peritapetal membrane between the tapetal cytoplasm and the adjacent middle layer of the anther wall. Furthermore, labelling was observed within the locule in association with globules resembling pro-Ubisch bodies which appeared at the tetrad stage. During the early vacuolate stage of microspore development the young exine was strongly labelled. The exine and the peritapetal membrane both are composed of sporopollenin, and the pro-Ubisch bodies are thought to contain sporopollenin precursors. Thus, SaTAP35 and SaTAP44 might be involved in sporopollenin formation and/or deposition.


Journal of Dairy Research | 2016

Functional and technological properties of camel milk proteins: a review

Yonas Hailu; Egon Bech Hansen; Eyassu Seifu; Mitiku Eshetu; Richard Ipsen; Stefan Kappeler

This review summarises current knowledge on camel milk proteins, with focus on significant peculiarities in protein composition and molecular properties. Camel milk is traditionally consumed as a fresh or naturally fermented product. Within the last couple of years, an increasing quantity is being processed in dairy plants, and a number of consumer products have been marketed. A better understanding of the technological and functional properties, as required for product improvement, has been gained in the past years. Absence of the whey protein β-LG and a low proportion of к-casein cause differences in relation to dairy processing. In addition to the technological properties, there are also implications for human nutrition and camel milk proteins are of interest for applications in infant foods, for food preservation and in functional foods. Proposed health benefits include inhibition of the angiotensin converting enzyme, antimicrobial and antioxidant properties as well as an antidiabetogenic effect. Detailed investigations on foaming, gelation and solubility as well as technological consequences of processing should be investigated further for the improvement of camel milk utilisation in the near future.


Plant Journal | 1994

A light‐ and temperature‐entrained circadian clock controls expression of transcripts encoding nuclear proteins with homology to RNA‐binding proteins in meristematic tissue

Christian Heintzen; Slegbert Melzer; Ruth Fischer; Stefan Kappeler; Klaus Apel; Dorothee Staiger


Biochemical and Biophysical Research Communications | 2006

Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk

Stefan Kappeler; Hans M. van den Brink; Henrik Rahbek-Nielsen; Z. Farah; Zdenko Puhan; Egon Bech Hansen; Eric Johansen


Journal of Dairy Science | 2004

Expression of the Peptidoglycan Recognition Protein, PGRP, in the Lactating Mammary Gland

Stefan Kappeler; C. Heuberger; Z. Farah; Zdenko Puhan


Journal of Dairy Science | 2003

5′-Flanking Regions of Camel Milk Genes Are Highly Similar to Homologue Regions of Other Species and Can be Divided into Two Distinct Groups

Stefan Kappeler; Z. Farah; Zdenko Puhan


Journal of Dairy Science | 1999

Alternative splicing of lactophorin mRNA from lactating mammary gland of the camel (Camelus dromedarius).

Stefan Kappeler; Z. Farah; Zdenko Puhan


International Dairy Journal | 1999

Sequence analysis of camel (Camelus dromedarius) lactoferrin

Stefan Kappeler; Manfred Ackermann; Z. Farah; Zdenko Puhan


Archive | 2001

Verfahren zur herstellung von nicht aus dem rind stammendem chymosin und dessen anwendung Process for the preparation of non-bovine derived from chymosin and its application

Stefan Kappeler; Zakaria Farah; Peter Budtz; Henrik Rahbek-Nielsen; Den Brink Johannes Maarten Van

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Z. Farah

École Polytechnique Fédérale de Lausanne

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Zdenko Puhan

École Polytechnique Fédérale de Lausanne

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Klaus Apel

École Polytechnique Fédérale de Lausanne

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Ruth Fischer

École Polytechnique Fédérale de Lausanne

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Slegbert Melzer

École Polytechnique Fédérale de Lausanne

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Egon Bech Hansen

Technical University of Denmark

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